HSP Proteins

Heat Shock Proteins and Molecular Chaperones
Heat Shock Proteins and Molecular Chaperones Antibodies Proteins ELISA Kits
Hsp10 Hsp27 Hsp32 Hsp40 Hsp60 Hsp70 Hsp90 Hsp110 Chaperones
Hsp10 ....................................3 Hsp27 ....................................3 Hsp32 ....................................5 Hsp40 and the DnaJ Family ...7 Hsp60 and GroEL ..................9 Hsp70 and DnaK.................11 Hsp90 ..................................13 Hsp110 ................................15 Chaperones & Others.........16 Hsp27 Review .....................20 Hsp70 Review .....................22 Hsp90 Review .....................24 References ..........................26
Assay Designs is committed to providing scientists with reliable tools for scientific discovery. Our merger in 2005 with Stressgen Bioreagents has broadened our product offering to include an extensive collection of heat shock protein related products including ELISA kits, antibodies, recombinant proteins, and reagents. We are pleased to add the high quality products generated by over 15 years of Stressgen research into our product line, and are dedicated to the further development and manufacturing of novel userfriendly heat shock protein related products. Assay Designs aims to Simplify Your Science by offering this guide to the heat shock protein families, and the products we offer to advance research in this existing field. Heat shock proteins are ubiquitously expressed polypeptides whose expression increases in response to a variety of different metabolic insults. Despite their designation, most of the heat shock proteins are constitutively expressed and perform essential functions. Most notable is their role as molecular chaperones, facilitating the synthesis and folding of proteins throughout the cell. In addition, heat shock proteins have been shown to participate in protein assembly, secretion, trafficking, protein degradation, and the regulation of transcription factors and protein kinases. Increased levels of the heat shock proteins after stress plays a central role in cellular homeostasis.
&
Species:
H: human M: mouse R: rat B: bovine C: chicken D: drosophila Y: yeast
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Bestellen in Deutschland: Biomol GmbH Fon: 0800-246 66 51 Fax: 0800-246 66 52 info@biomol.de www.biomol.de Technischer Support: ts@biomol.de
Applications:
WB: western blot IP: immunoprecipitation ICC: immunocytochemistry IHC: immunohistochemistry F: flow cytometry
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Hsp10
Hsp10, also known as Chaperonin 10 (Cpn10), is the ~10 kDa mammalian equivalent of the bacterial GroES gene product. Hsp10 exists in vivo as an oligomer and interacts with Hsp60, the mammalian homolog of the bacterial GroEL protein. Together the Hsp10/Hsp60 chaperonin present within mitochondria facilitates the folding of newly synthesized proteins and may participate in the refolding of proteins damaged after stress. In plants, a similar chaperonin system operates within chloroplasts and is referred
Entrez Gene ID
3336
Assay Designs (Stressgen) Products

Cat. No. SPA-110 SPA-210 SPP-620 Product Description Hsp10 (Cpn10) Polyclonal Antibody GroES Polyclonal Antibody GroES Recombinant Protein Species H, M, R, X E.coli E.coli Application WB, IP WB, IP
to as the Rubisco-Binding protein. Finally, in bacteria GroEL and GroES participate in the folding and assembly of numerous proteins.
Tissue Distribution
Broad
Official Symbol
HSPE1
Name
Heat Shock 10kDa Protein 1 (Chaperonin 10)
Synonyms
CPN10, GROES, HSP10
Biological Function
Caspase activation, Chaperone binding, Protein folding
Cellular Distribution
Mitochondria Chloroplasts
Hsp27
Hsp27 (sometimes referred to as Hsp20, Hsp25, Hsp28 or the low molecular weight heat shock protein) is homologous to the a Crystallin proteins. Both families of proteins are characterized by their oligomeric structure and are thought to function as ATP-independent chaperones. Hsp27 structure/function is thought to be modulated by phosphorylation mediated by different protein kinases. In addition to their chaperone role, Hsp27 and aB-Crystallin have been shown to mediate structural integrity and membrane stability, affecting actin polymerization, intermediate filament organization, apoptosis, and invasive potential. Evidence suggests altered expression of small heat shock proteins is implicated in the pathogenesis of human diseases including cancer, cataracts, neurodegenerative disorders, and cardiovascular disease.
Cat. No. EKS-500 SPA-796 SPA-801 SPA-803 SPA-800 SPA-525 SPA-523 SPA-524 905-642 SPA-800FI SPA-800B SPA-221 SPA-222 SPA-223 SPA-224 SPA-225 SPA-226 SPA-227 SPA-230 NSP-510 SPP-715 ESP-715 SPP-226 SPP-227 SPP-225 Product Description Hsp27 ELISA Kit Hsp20 Polyclonal Antibody Hsp25 Polyclonal Antibody Hsp27 Polyclonal Antibody Hsp27 Monoclonal Antibody (G3.1) Hsp27 (phospho-Ser15) Polyclonal Antibody Hsp27 (phospho-Ser78) Polyclonal Antibody Hsp27 (phospho-Ser82) Polyclonal Antibody Hsp27 (phospho-Ser82) Monoclonal Antibody Hsp27 Monoclonal Antibody, FITC Conjugate Hsp27 Monoclonal Antibody, Biotin Conjugate a A Crystallin Polyclonal Antibody a B Crystallin Monoclonal Antibody a B Crystallin Polyclonal Antibody a A/B Crystallin Polyclonal Antibody
Hsp27 Review on page 20
Species H H, M, R M, R H H, M, R H, M, R H, M, R H, R H, M, R H, M, R H, M, R B H, M, R, B, C H, M, R, B B H, M, B H, M, R, B, C, X M, R, B B M H H B B B
Application
WB WB, IP, ICC, IHC WB, IP, ICC, IHC WB, IP, ICC, IHC WB WB, IP WB, IP WB F, IF
WB, IP WB, ICC, IHC WB, IP WB WB, IP WB, IP WB, IP WB
a B Crystallin (phospho-Ser19) Polyclonal Antibody a B Crystallin (phospho-Ser45) Polyclonal Antibody a B Crystallin (phospho-Ser59) Polyclonal Antibody b Crystallin Monoclonal Antibody (3H92) Hsp25 Recombinant Protein Hsp27 Recombinant Protein Hsp27 Recombinant Protein - Low Endotoxin a A Crystallin Native Protein a B Crystallin Native Protein a A/B Crystallin Native Protein
03
Hsp27 (continued)
Official Symbol
CRYAA CRYAB
Name
Crystallin, a A Crystallin, a B
Synonyms
CRYA1, HSPB4 CRYA2, HSPB5
Entrez Gene ID
1409 1410
Biological Function
Structural component of eye, Protein Folding Structural component of eye, Protein Folding, Muscle contraction, Muscle development, Protein folding, Receptor mediated signaling, Visual perception Anti-apoptosis, Cell motility, Protein folding
Tissue Distribution
Eye Lens Broad
Cellular Localization
Cytoplasm Contractile fibers, Cytoplasm, Nucleus, Plasma membrane Cytoplasm Nucleus, Plasma Membrane
Human Diseases
Cataracts Cataracts, Multiple Sclerosis
HSPB1
Heat Shock 27kDa Protein 1
HSP27, Hsp25
3315
Broadly
Charcot-MarieTooth disease, axonal, type 2F. Neuropathy, distal hereditary motor
HSPB2 HSPB3 HSPB6
Heat Shock 27kDa Protein 2 Heat Shock 27kDa Protein 3 Heat Shock Protein, a-Crystallinrelated, B6 Heat Shock 27kDa Protein family, member 7 (cardiovascular) Heat Shock 22kDa Protein 8
MKBP HSPL27 Hsp20
3316 8988 126393
Enzyme Activator, Protein Folding, Somatic Muscle Development Protein Folding Structural component of eye, Protein Folding, Muscle Contraction Protein Folding, Muscle Contraction
Heart, Skeletal Muscle, Skin Muscle Muscle, Ovary
Cytoplasm, Nucleus
Actin cytoskeleton Contractile Fibers
HSPB7
cvHSP
27129
Cardiac, Connective, Skeletal Broadly
HSPB8
H11; E2IG1; HSP22
26353
Kinase Activity, Transferase Activity, Protein Folding
Cytoplasm, Plasma Membrane
CharcotMarie-Tooth disease type 2L. Hereditary motor neuropathy type II
HSPB9
Heat Shock Protein, a-Crystallinrelated, B9 Outer dense fiber of sperm tails 1 HSPB10, ODFP, SODF
94086
Protein Folding
Testes
Nucleus, Cytoplasm Cytoplasm
ODF1
4956
Structural activity, Cell differentiation, Spermatogenesis
Testes
Hsp27 (phospho-Ser82) Polyclonal Antibody (Cat. No. SPA-524)

Confocal immunofluorescent staining of Hela cells using Phospho-Hsp (Ser82) Polyclonal Antibody (Cat. No. SPA-524; green) (A). Blue pseudocolor fluorescent dye DRAQ5 was used to stain cell nuclei (B). In (C) the two images are overlapped.
04
H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast
Hsp32 (Heme Qxygenase)

Heme oxygenase or Hsp32 is an esCat. No. Product Description Species Application sential component in the catabolism of heme, catalyzing the first step in EKS-800 HO-1 (Hsp32; Human) ELISA Kit H the degradation of heme to bilirubin. EKS-810 HO-1 (Hsp32; Rat) ELISA Kit R Heme oxygenase consists of at least SPA-895 HO-1 (Hsp32) Polyclonal Antibody H, M, R WB, IP, ICC, IHC, F three isoforms: stress inducible HO-1, SPA-896 HO-1 (Hsp32) Polyclonal Antibody H, M, R WB, IP, ICC, IHC and constitutively expressed HO-2 OSA-150 HO-1 (Hsp32) Polyclonal Antibody H, M, R WB, IP and HO-3. Induction of HO-1 occurs OSA-110 HO-1 (Hsp32) Monoclonal Antibody (HO-1-1) H, M, R WB, F in response to heat shock, oxidative OSA-111 HO-1 (Hsp32) Monoclonal Antibody (HO-1-2) H, M, R WB, IHC, F stress, thiol reacting reagents, heavy OSA-111FI HO-1 (Hsp32) Monoclonal Antibody-FITC Conjugate H, M, R F, IF metals, inflammatory mediators and OSA-111B HO-1 (Hsp32) Monoclonal Antibody-Biotin Conjugate H, M, R certain growth factors. The majoOSA-200 HO-2 Polyclonal Antibody H, M, R WB rity of the protein is localized to SPA-897 HO-2 Polyclonal Antibody H, M, R, C WB, IP, ICC the endoplasmic reticulum, but the SPP-730 HO-1 (Hsp32) Recombinant Protein R protein can also be present at the plasma membrane and mitochondSPP-732 HO-1 (Hsp32) Recombinant Protein H ria. The products produced by heme NSP-550 HO-2 Recombinant Protein H oxygenase have important physiological effects: carbon monoxide is a potent vasodilator; biliverdin and its product bilirubin are antioxidants; and the released iron can increase oxidative stress if not effectively reutilized. Modulation of HO expression may be useful for protection against atherosclerotic disease, oxidative stress, coronary ischemia, hypertension and certain neurodegenerative diseases.
Official Symbol
HMOX1 HMOX2
Name
Heme Oxygenase 1 Heme Oxygenase 2
Synonyms
HO-1 HO-2
Entrez Gene ID
3162 3163
Biological Function
Breakdown of heme, protection against oxidative stress, Ion binding, NFkB signaling Breakdown of heme, protection against oxidative stress, Electron carrier, Ion binding
Tissue Distribution
Broad Broad
Endoplasmic reticulum Endoplasmic reticulum
Heme-Oxygenase-1 (Hsp32) Monoclonal Antibody (Cat. No. OSA-111)

Human lung carcinoma tissue was immunohistochemically stained using Heme-Oxygenase-1 Monoclonal Antibody (clone HO-1-2) at a dilution of 1:50. Another Heme-Oxygenase-1 monoclonal (clone HO-1-1, Cat. No. OSA-110) (1:50) was negative for staining the same lung cancer tissue.
WB: western blot, IP: immunoprecipitation, ICC: immunocytochemistry, IHC: immunohistochemistry, F: flow cytometry
05
Hsp32 (continued)
Heme Oxygenase 1 (Hsp32)

Crystal structure of human Heme Oxygenase-1 in complex with its substrate Heme (Schuller, D.J. et al. 2002).
Heme-Oxygenase-1 (Hsp32) Monoclonal Antibody (Cat. No. OSA-110)

Human lung cancer A2 cells were analyzed by flow cytometry using isotype control antibody (left) or Heme-Oxygenase-1 Monoclonal Antibody (clone HO-1-1; right) at a final concentration of 10g/mL.
06
Hsp40 and the DnaJ Family

Mammalian Hsp40, present within the cytosol, is one Assay Designs (Stressgen) Products of a number of family members closely related to Cat. No. Product Description Species Applications the DnaJ protein first described in E.coli. Hsp40/DnaJ SPA-400 Hsp40 Polyclonal Antibody H, M, R, C, X WB, IP, ICC, IHC family members work in concert with the Hsp70/DnaK SPA-450 Hsp40 Monoclonal Antibody (2E1) H, M, R WB, IP proteins, facilitating the hydrolysis of ATP to ADP and SPA-410 DnaJ Polyclonal Antibody E. coli WB, IP thereby helping to lock in the binding of the Hsp70 SPP-400 Hsp40 Recombinant Protein H chaperone to its protein substrate. Consequently, SPP-640 Active DnaJ Recombinant Protein E. coli each of the different members of the Hsp70 family in eukaryotes require a specific DnaJ homolog for their chaperone activity. More than 20 genes encoding DnaJrelated proteins have been identified in yeast. In animal cells the Hsp40 family of proteins display a broad tissue distribution with individual members present within most intracellular compartments. Assay Designs currently provides both the DnaJ and Hsp40 proteins in purified form, along with a number of antibodies specific for each protein. New products targeting other members of the DnaJ/Hsp40 family are expected in the near future.
Official Symbol
DNAJA1
Name
DnaJ (Hsp40) homolog, subfamily A, member 1
Synonyms
DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; hDJ-2
Entrez Gene ID
3301
Biological Function
Protein binding, Protein folding, LDL receptor binding, Ion binding
Tissue Distribution
Broadly
Cytoplasm Nucleus Nucleolus Golgi Cytoplasm Nucleus Mitochondrion Mitochondrion
DNAJA2
DnaJ (Hsp40) homolog, subfamily A, member 2 DnaJ (Hsp40) homolog, subfamily A, member 3 DnaJ (Hsp40) homolog, subfamily A, member 4 DnaJ homology subfamily A, member 5 DnaJ (Hsp40) homolog, subfamily B, member 1 DnaJ (Hsp40) homolog, subfamily B, member 2 DnaJ (Hsp40) homolog, subfamily B, member 4 DnaJ (Hsp40) homolog, subfamily B, member 5 DnaJ (Hsp40) homolog, subfamily B, member 6 DnaJ (Hsp40) homolog, subfamily B, member 7 DnaJ (Hsp40) homolog, subfamily B, member 8 DnaJ (Hsp40) homolog, subfamily B, member 9
CPR3; DJA2; DNAJ; DNJ3; RDJ2; HIRIP4 TID1, hTid-1
10294
Protein binding, Ion binding, Cell cycle, Protein Folding GTPase activity, Ion Binding, GPCR Signaling, Protein folding, Protein folding, Regulation of apoptosis Protein binding, Ion binding, Protein folding Protein binding, Nucleic acid binding, Ion binding, Protein folding Protein binding, Protein Folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein Binding, Protein folding Protein binding, Protein folding Chaperone, Protein folding, activity, Protein binding
Broadly
DNAJA3
9093
Broad
DNAJA4 DNAJA5 DNAJB1 DNAJB2 DNAJB4 DNAJB5 DNAJB6 DNAJB7 DNAJB8 DNAJB9
MST104; MSTP104; PRO1472 GS3 protein Hdj1; HSPF1; Hsp40 HSJ1; HSPF3 DjB4; HLJ1; DNAJW Hsc40 MRJ; HSJ2; HHDJ1; HSJ-2; MSJ-1 HSC3 MGC33884 MDG1; ERdj4
55466 134218 3337 3300 11080 25822 10049 150353 165721 4189
Broad Broad Broad Broad Broad Broad Broad Broad Cytoplasm Nucleus Cytoplasm Nucleus Nucleus Cytoplasm Nucleus
Broad
Cytoplasm Endoplasmic reticulum Nucleolus Nucleus Cytoplasm Endoplasmic reticulum Nucleus
DNAJB11
DnaJ (Hsp40) homolog, subfamily B, member 11
EDJ; ERj3; HEDJ; hDj9; ABBP2; ERdj3; ABBP-2
51726
Protein binding, Protein folding
Broad
datasheet: www.biomol.de www.antibodyworld.com
07
Hsp40 (continued)
Official Symbol DNAJB12 DNAJB13 DNAJB14 DNAJC1 Name DnaJ (Hsp40) homolog, subfamily B, member 12 DnaJ (Hsp40) related, subfamily B, member 13 DnaJ (Hsp40) homolog, subfamily B, member 14 DnaJ (Hsp40) homolog, subfamily C, member 1 HTJ1; ERdj1; DNAJL1 Synonyms DJ10 TSARG5; TSARG6 Entrez Gene ID 54788 374407 79982 64215 Biological Function Protein binding, Protein folding Protein binding, Apoptosis, Protein folding, Spermatogenesis Protein binding, Protein folding ATPase activation, Protein folding, Chaperone folding, DNA binding Endoplasmic reticulum Membrane Microsome Nucleus Nucleus Testis Tissue Distribution Cellular Distribution Plasma membrane
DNAJC2
DnaJ (Hsp40) homolog, subfamily C, member 2 DnaJ (Hsp40) homolog, subfamily C, member 3 DnaJ (Hsp40) homolog, subfamily C, member 4 DnaJ (Hsp40) homolog, subfamily C, member 5 DnaJ (Hsp40) homolog, subfamily C, member 5 b DnaJ (Hsp40) homolog, subfamily C, member 5 g DnaJ (Hsp40) homolog, subfamily C, member 6 DnaJ (Hsp40) homolog, subfamily C, member 7 DnaJ (Hsp40) homolog, subfamily C, member 8 DnaJ (Hsp40) homolog, subfamily C, member 9 DnaJ (Hsp40) homolog, subfamily C, member 10 DnaJ (Hsp40) homolog, subfamily C, member 11 DnaJ (Hsp40) homolog, subfamily C, member 12 DnaJ (Hsp40) homolog, subfamily C, member 13 DnaJ (Hsp40) homolog, subfamily C, member 14 DnaJ (Hsp40) homolog, subfamily C, member 15 DnaJ (Hsp40) homolog, subfamily C, member 16 DnaJ (Hsp40) homolog, subfamily C, member 17 DnaJ (Hsp40) homolog, subfamily C, member 18 DnaJ (Hsp40) homolog, subfamily C, member 19 HscB iron-sulfur cluster co-chaperone homolog (E. coli) HscB iron-sulfur cluster co-chaperone homolog (E. coli)
Zrf1; Zrf2; MIDA1
22791
DNA binding, Cell cycle, Protein binding, DNA replication, Protein folding, Transcription Protein binding, Protein folding, Kinase inhibitor, Defense Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Signal transduction, Hydrolase activity, Protein folding, Phosphatase activity Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Redox homeostasis, Protein folding Protein binding, Protein folding Protein binding , Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding Protein binding, Protein folding RNA binding, Protein folding, Protein binding Protein binding, Protein folding Protein binding, Protein folding, Protein transport Chaperone binding, Protein binding, Protein folding Broad Broad Broad Broad Broad Broad Broad Broad Broad Pituitary Gland Broad
DNAJC3 DNAJC4 DNAJC5 DNAJC5B DNAJC5G DNAJC6
P58; HP58; PRKRI; P58IPK HSPF2; MCG18; DANJC4 CSP CSP-b CSP-g DJC6
5611 3338 80331 85479 285126 9829
Cytoplasm Membrane Membrane
Membrane Nucleus
DNAJC7 DNAJC8 DNAJC9 DNAJC10 DNAJC11 DNAJC12 DNAJC13 DNAJC14 DNAJC15 DNAJC16 DNAJC17 DNAJC18 DNAJC19 DNAJC20
TPR2; TTC2; DANJC7 SPF31; HSPC331 JDD1; SB73 JPDI; ERdj5
7266 22826 23234 54431 55735
Nucleolus
Endoplasmic Reticulum Mitochondrion
JDP1 RME8 DNAJ; HDJ3; LIP6 MCJ; HSD18; DNAJD1
56521 23317 85406 29103 23341 55192 202052
Endosome Endoplasmic reticulum
Membrane
Membrane Membrane Mitochondrion Mitochondrion
TIM14; TIMM14 HSCB, JAC1; HSC20
131118 150274
HSCB
DNAJC20
150274
08
Hsp47 Monoclonal Antibody (Cat. No. SPA-470)

Human breast cancer tissue was immunohistochemically stained using Hsp47 Monoclonal Antibody (clone M16.10A1) at a dilution of 1:50.
Hsp60 and GroEL: the Chaperonins

Members of the Hsp60 (eukaryotes) and GroEL (bacterial) family of heat shock proteins are some of the best characterized molecular chaperones. Bacterial GroEL, named because of its essential role in bacteriophage growth, exists as a large homo-oligomeric complex which recognizes and binds to unfolded polypeptides. In combination with its particular co-factor (Hsp10 in eukaryotes, GroES in bacteria) the Hsp60/ GroEL proteins bind newly synthesized polypeptides and facilitate their folding to the native state via one or more rounds of ATP hydrolysis. Mammalian Hsp60 is localized within mitochondria, while a related form of the protein termed Rubisco-binding protein operates within plant chloroplasts. Finally, within the eukaryotic cytosol, related proteins referred to as CCT or TRIC make a hetero-oligomeric structure and have been shown to similarly bind select protein substrates and facilitate their folding and/or higher order assembly. Oftentimes the GroEL/ES or Hsp60/Hsp10 protein folding machineries are referred to as the chaperonins. In vitro as well as in vivo chaperonins, either alone or with other chaperones and ATP, have been shown to orchestrate the re-folding of partially denatured proteins. In addition to their prominent role as molecular chaperones members of the GroEL and Hsp60 families have long been recognized as

Cat. No. EKS-600 EKS-650 SPA-807 SPA-806 SPA-829 SPA-828 SPA-881 SPS-870 SPS-875 SPA-110 SPA-210 CTA-123 CTA-191 CTA-202 ESP-540 Product Description Hsp60 ELISA Kit (measures protein) Hsp60 ELISA Kit (measures antibodies) Hsp60 Monoclonal Antibody (LK-2) Hsp60 Monoclonal Antibody (LK-1) Hsp60 Monoclonal Antibody (11-13) Hsp60 Goat Polyclonal Antibody Hsp65 Monoclonal Antibody (3F7) GroEL Monoclonal Antibody (9A1/2) GroEL Polyclonal Antibody Hsp10 (Cpn10) Polyclonal Antibody GroES Polyclonal Antibody TCP-1a Monoclonal Antibody (23c) TCP-1a Monoclonal Antibody (91a) TCP-1b Monoclonal Antibody Active Hsp60 Recombinant Protein (Low Endotoxin) NSP-540 ESP-741 Active Human Hsp60 Recombinant Protein Active Mouse Hsp60 Recombinant Protein (Low Endotoxin) SPP-741 SPP-742 NSP-581 SPP-610 SPP-620 Hsp60 Recombinant Protein Hsp60 Recombinant Protein Hsp65 Recombinant Protein Active GroEL Recombinant Protein GroES Recombinant Protein M R Mycobacterim E. coli E. coli H M Species H H H, M, R, C, Y H, M, R, C, X H, M, R, D H, M, R, C, X H, M, R, D E. coli H, M, R, Y, E. coli H,,M, R, X E. coli M, R H, M, R, D, Y H, M, R, C H WB, IHC, F WB, IP, F WB, IP, IHC, F WB, IP WB WB, IP WB W, IP W, IP W, IP, ICC WB, IP, F WB Applications
09
Hsp60 (continued)
highly immunogenic proteins and consequently have attracted much attention from immunologists. Assay Designs offers a comprehensive panel of both purified chaperonin proteins isolated from different sources along with antibodies capable of discerning the different family members.
Official Symbol
HSPD1
Name
Heat Shock 60kDa Protein 1 (chaperonin)
Synonyms
CPN60; GROEL; HSP60; HSP65; SPG13; HuCHA60
Entrez Gene ID
3329
Biological Function
Protein folding, Nucleotide binding, Protein import, Regulation of apoptosis
Tissue Distribution
Broad
Mitochondrion Cytoplasm
Human Diseases
Spastic paraplegia

Human colon cancer tissue was immunohistochemically stained using Hsp60 Monoclonal Antibody (clone LK-2) at a dilution of 1:50.

Human hepatoma tissue was immunohistochemically stained using Hsp60 Monoclonal Antibody (clone LK-1) at a dilution of 1:50. Another Hsp60 monoclonal (clone 11-13, Cat. No. SPA-806) (1:50) was negative for staining the same hepatoma tissue.

Human hepatoma QGY cells were analyzed by flow cytometry using isotype control antibody (left) or Hsp60 Monoclonal Antibody (clone LK-1; right) at a final concentration of 10g/mL.
10
Hsp70 and DnaK

The Hsp70 family of heat shock proteins contains multiple homologues ranging in size from 66kDa to 78kDa. These proteins include cognate members which are found within major intracellular compartments, and highly inducible isoforms which are predominantly cytoplasmic or nuclear in distribution. All Hsp70 family members contain a highly conserved N-terminal ATPase domain, as well as a conserved hydrophobic peptide binding domain (PBD) and more variable a-helical cap domain. Activation of Hsp70 is coordinated by binding of ATP at the N-terminus, causing a conformational change that opens the cap, allowing interaction of the PBD with a wide variety of client proteins in their unfolded, misfolded, or denatured state. Hsp70 ATPase activity is influenced by association with

specific co-chaperone molecules, including Hsp40, Hip, Hop, Hup, Hap, and CHIP. These co-chaperones cooperate with Hsp70 to fold newly synthesized proteins, re-fold misfolded or denatured proteins, coordinate trafficking of proteins across cellular membranes, disassemble clathrin-coated vesicles, inhibit protein aggregation, and target the degradation of proteins via the proteasomal pathway. Elevated levels of Hsp70 have been associated with inhibition of apoptosis, and clinical correlations between Hsp70 expression and poor cellular differentiation, increased lymph node metastasis, chemoresistance, and poor clinical outcome indicate Hsp70 may be of use in the diagnosis, prognosis, and treatment of human malignancy.

Cat. No. EKS-700 EKS-750 EKS-725 SPA-810 SPA-810FI SPA-810B SPA-812 SPA-811 SPA-820 SPA-822 SPA-757 SPA-815 SPA-816 SPA-756 SPA-754 SPA-766 SRA-1500 SPS-825 SPA-826 NSP-555 ESP-555 SPP-758 SPP-751 SPP-752 Product Description Hsp70 ELISA Kit (assay protein) Hsp70 ELISA Kit (assay antibodies) Hsp70B ELISA Kit (assay protein) Hsp70 (Hsp72) Monoclonal Antibody (C92F3A-5) Hsp70 (Hsp72) Monoclonal Antibody, FITC Conjugate Hsp70 (Hsp72) Monoclonal Antibody, Biotin Conjugate Hsp70 (Hsp72) Polyclonal Antibody Hsp70 (Hsp72) Polyclonal Antibody Hsp70/Hsc70 Monoclonal Antibody (N27F3-4) Hsp70/Hsc70 Monoclonal Antibody (BB70) Hsp70/Hsc70 Polyclonal Antibody Hsc70 (Hsp73) Rat Monoclonal Antibody (1B5) Hsc70 (Hsp73) Polyclonal Antibody Hsp70B Polyclonal Antibody Hsp70B Monoclonal Antibody (175f) Hip Polyclonal Antibody HOP (p60) Monoclonal Antibody (DS14F5) Grp75 Monoclonal Antibody (30A5) Grp78 (BiP) Polyclonal Antibody Active Hsp70 (Hsp72) Recombinant Protein Active Hsp70 Recombinant Protein (Low Endotoxin) Active Hsp70 (Hsp72) Recombinant Protein Active Hsc70 (Hsp73) Recombinant Protein Active Hsc70 (Hsp73) Recombinant Protein, ATPase fragment ESP-502 Active Hsp70-A2 Recombinant Protein (Low Endotoxin) SPP-762 SPP-767 SRP-1510 SPP-765 Hsp70B Recombinant Protein Hip Recombinant Protein HOP (p60) Recombinant Protein Grp78 (BiP) Recombinant Protein H R H Hamster M Species H, M, R H H H, M, R, C, D H, M, R, C, D H, M, R, C, D H, M, R, F H, M, R H, M, R, C, X H, M, R, C, X H, M, R, C, Y H, M, R, C H, M, R H H H, M, R, B H, M, R, C, X H, M, R, C, D, X M, R, X H H R B B WB, IP, ICC, IHC WB WB, F WB, IHC, F WB, IP WB, IP, ICC, IHC, F WB, ICC, IHC WB, IP WB WB WB, IP WB, IHC WB, IP, ICC, IHC WB, IHC, F Applications
11
Hsp70 (continued)
Official Symbol HSPA1A Name Heat Shock 70kDa Protein 1A Synonyms HSP72, HSPA1, HSPA1B, HSP70-1 Entrez Gene ID 3303 Biological Function Nucleotide binding, Protein folding Tissue Distribution Broadly Cellular Distribution Cytoplasm, Nucleolus Human Diseases Alzheimers, Ankylosing spondylitis, Asthma, Chronic obstructive pulmonary , Multiple sclerosis, Parkinsons disease, Restenosis, Schizophrenia, Tuberculosis Asthma, Alzheimers, Obesity, Chronic obstructive pulmonary, Crohns disease, Diabetes (type 1 & 2), Hypothyroidism, Multiple, Pancreatitis, Parkinsons disease, Schizophrenia, Sclerosis, Restenosis Chronic obstructive pulmonary disease, Graft vs. Host disease, Hypothyroidism, Multiple sclerosis, Parkinsons disease, Restenosis, Schizophrenia, Septic shock, Storke Alzheimers, Crohns, Sepsis
HSPA1B
Heat Shock 70kDa Protein 1B
HSP70-2
3304
Nucleotide binding, Protien folding, Regulation of apoptosis
Broad?
Cytoplasm, Endoplasmic reticulum, Mitochondrion Nucleus Cytoplasm, Nucleus
HSPA1L
Heat Shock 70kDa Protein 1-like
Hum70t, HSP70-HOM
3305
Nucleotide binding, DNA repair, Protein folding, Telomere maintenance
Broad?
HSPA2
Heat Shock 70kDa Protein 2 Heat Shock 70kDa Protein 4 RY, APG2, Hsp70, Hsp70RY, HS24/P52 BIP, MIF2, GRP78
3306
Nucleotide binding, Protein folding, Spermatogenesis Nucleotide binding, Protein folding
Broad
Nucleus, Cytoplasm, Nucleolus Cytoplasm
HSPA4
3308
Broad
Preterm delivery, Carotid Plaques
HSPA5
Heat Shock 70kDa Protein 5 (glucose-regulated protein, 78kDa) Heat Shock 70kDa Protein 6 (HSP70B) Heat Shock 70kDa Protein 7 (HSP70B) Heat Shock 70kDa Protein 8
3309
Nucleotide binding, Apoptosis, Caspase regulation, Protein binding, Ribosome binding
Broad
Endoplasmic Reticulum, Plasma Membrane, Cytoplasm, Nucleolus, Nucleus
Bipolar disease, Schizophrenia
HSPA6
3310
Nucleotide binding, Protein folding Nucleotide binding, rotein folding Nucleotide binding, Protein folding, ATPase activity Broad
HSPA7
HSP70B
3311
HSPA8
LAP1, HSC54, HSC70, HSC71, HSP71, HSP73, NIP71, HSPA10 CSA, MOT, MOT2, GRP75, HSPA9, PBP74, Mot-2 HSP70-4; HSP70L1
3312
Cytoplasm, Nucleus
Cystic Fibrosis, Lung cancer
HSPA9
Heat Shock 70kDa Protein 9 (Mortalin) Heat Shock 70kDa Protein 14
3313
Nucleotide binding, Protein folding, Regulation of apoptosis
Cytoplasm Mitochondria
HSPA14
51182
Hsp70
Substrate binding domain of Hsp70 in complex with a substrate peptide. Science (1996) 272(5268):1606-1614.

Human colon cancer tissue was immunohistochemically stained using Hsp70 Monoclonal Antibody (clone C92F3A-5) at a dilution of 1:50.
12
Hsp90
The 90kDa molecular chaperone family comprises several proteins including the 90 kDa heat shock protein Hsp90 and the 94kDa glucose-regulated protein grp94, which are major molecular chaperones of the cytosol and endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and Hsp90b, which are encoded by separate genes. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions which contain independent chaperone sites with different client protein specificity. Hsp90 is part of the cells network of chaperones that regulate protein folding and assembly, requiring both ATP and co-chaperones (e.g. Hsp70, Hsp40, Hip/Hop, p23, and Aha1) for function. Inhibition of the Hsp90 protein folding

machinery targets client proteins for ubiquitin-mediated proteolysis. Hsp90 is also a necessary component of fundamental cellular processes such as hormone signaling, cell growth, and differentiation through its binding of client proteins such as ErbB2/Her-2, Akt, Raf, CDK1, and CDK4. In addition to its homeostatic and stress induced roles in protein folding, grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presenting cells. Strategies seeking to disrupt Hsp90 activation of key pro-survival pathways hold promise as either direct or adjuvant therapies for cancers displaying altered Hsp90 expression.

Cat. No. EKS-895 SPA-830 SPA-835 SPA-845 SPA-846 SPS-771 SPA-840 SPA-843 SPA-842 SRA-1400 SPA-670 SPP-776 SPP-770 SPP-670 HPK-102 HPK-101 Product Description Hsp90a ELISA kit Hsp90 Monoclonal Antibody (AC88) Hsp90 Rat Monoclonal Antibody (16F1) Hsp90 Rat Monoclonal Antibody (2D12) Hsp90 Polyclonal Antibody Hsp90a Polyclonal Antibody Hsp90a Rat Monoclonal Antibody (9D2) Hsp90b Monoclonal Antibody (K3701) Hsp90b Monoclonal Antibody (K3705) FKBP-59 (Hsp56, p59) Monoclonal Antibody p23 Polyclonal Antibody Hsp90a Recombinant Protein Hsp90 Native Protein p23 Recombinant Protein Geldanamycin 17-AAG Species H H, M, R, C H, M, R, C, D H, M, R, C H, M, R, C H, M, R, C, X H, C H, M, R H, M, R, C H, M, R H, M, R H H H WB, IP, ICC, IHC, F WB, IP, ICC, IHC WB, IP WB WB, IP WB, IHC, F WB, F WB, IHC WB, IP, ICC, IHC WB Applications
Official Symbol HSP90AA1
Name Heat Shock Protein 90kDa a (cytosolic), class A member
Synonyms HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP90A; HSP90N; HSPCAL1; HSPCAL4 HSP90ALPHA, HSPCA, HSPCAL3 HSPC2; HSPCB; D6S182; HSP90B; FLJ26984; HSP90-BETA GP96; GRP94
Entrez Gene ID 3320
Biological Function Nucleotide binding, Protein folding, Protein dimerization, Signal transduction
Tissue Distribution Broadly
Cellular Distribution Cytoplasm, Nucleus
Human Diseases
HSP90AA2
Heat Shock Protein 90kDa a (cytosolic), class A member 2 Heat Shock Protein 90kDa a (cytosolic), class B member 1 Heat Shock Protein 90kDa b (Grp94), member 1
3324
Nucleotide binding, Protein folding Nucleotide binding, Protein folding Ion binding, Anti-apoptosis, Nucleotide binding, Ion sequestration , Protein folding, Protein transport Broad Cytoplasm
HSP90AB1
3326
HSP90B1
7184
Broad
Endoplasmic reticulum
Ischemic neuronal cell death
13
Hsp90 (continued)
Hsp90
Crystal structure of an Hsp90-Sba1 closed chaperone complex. Nature (2006) 440(7087):1013-1017.
Hsp90a Monoclonal Antibody (Cat. No. SPA-840)

Human colon cancer tissue was immunohistochemically stained using Hsp90a monoclonal antibody (clone 9D2) at a dilution of 1:50.
Hsp90b Monoclonal Antibody (Cat. No. SPA-842)

Human breast cancer tissue was immunohistochemically stained using Hsp90b monoclonal antibody (clone K3705) at a dilution of 1:50.
14
Hsp90a Monoclonal Antibody (Cat. No. SPA-840)

Human colon cancer Coca-2 cells were analyzed by flow cytometry using isotype control antibody (left) or Hsp90a monoclonal antibody (clone 9D2; right) at a final concentration of 10g/mL.
Hsp110
Hsp110 belongs to a family of large stress proteins referred to as the Hsp110/SSE (yeast stress seventy) family. Mammalian Hsp110 shares approximately 30% amino acid identity with its distant relative Hsp70, primarily in the conserved ATP-binding domain. Hsp110 is one of the three or four most abundant Hsps in mammalian tissue, with the highest constitutive expression in the brain. Functionally, Hsp110 appears to complex with other chaperones (predominantly Hsp70 and Hsp25) to maintain and repair protein folding. Hsp110 is more efficient than Hsp70 in conferring heat resistance, and has been shown to possess RNA-binding properties via the N-terminal ATPbinding domain. Due to the inherent efficiency of Hsp110 in binding peptide, the molecule has been utilized extensively as an immunoadjuvant to deliver known tumor antigens to antigen presenting cells, generating antigen-specific innate and adaptive anti-tumor responses.

Cat. No. SPA-1101 SPA-1103 Product Description Hsp110 Polyclonal Antibody Hsp110 Polyclonal Antibody Species H, M, R, B, Y H, M, R, B, X Applications WB, IP WB
Official Symbol HSPH1
Name Heat Shock 105kDa/ 110kDa Protein 1
Synonyms HSP105, HSP105A, HSP105B
Entrez Gene ID 10808
Biological Function Nucleotide binding, Protein binding
Tissue Distribution Protein folding
Cellular Distribution Broad
Human Diseases Cytoplasm
15
Chaperones & Others

The homeostatic process of protein folding and the protective functions of the protein folding machinery in stress-induced conditions (i.e. heat, starvation, oxidation) are dependent on heat shock proteins, as well as a diverse group of co-chaperones and transcriptional regulators. These molecules include the Hsp70 co-chaperones HIP and HOP, the ER resident chaperones Calnexin and Calreticulin, and Protein DisulfideIsomerase (PDI). ER-resident chaperones are folded in the ER, and retained via their KDEL peptide motif which is bound by the KDEL receptor (Erd2p). Together with the Hsps, these molecules participate in proper glycoprotein folding, prevent premature oligomerization of nascent proteins, regulate Hsp co-chaperone substrate specificity, and promote the rearrangement of disulphide bonds in the secretory pathway.

Cat. No. SPA-860 SPA-865 SPA-600 SPA-601 VAP-SV003 SPA-585 SPA-725 SPS-720 SRA-1400 SPA-240 SPA-766 SRA-1500 SPA-950 SPA-901 SPA-960 SPA-470 SPA-1040 SPA-827 VAA-PT048 VAM-PT046 SPA-670 SPA-890 SPA-891 VAM-SV021 CTA-123 CTA-191 CTA-202 VAP-PT068 SPP-767 SRP-1510 SPP-900 NSP-535 SPP-650 SPP-670 LYC-HL101 Product Description Calnexin Polyclonal Antibody Calnexin Polyclonal Antibody Calreticulin Polyclonal Antibody Calreticulin Monoclonal Antibody CSP Polyclonal Antibody ERp57 (Grp58) Polyclonal Antibody ERp57 (Grp58) Monoclonal Antibody ERp72 Polyclonal Antibody FKBP59 (Hsp56, p59) Monoclonal Antibody GrpE Polyclonal Antibody Hip Polyclonal Antibody HOP (p60) Monoclonal Antibody HSF-1 Rat Monoclonal Antibody HSF-1 Polyclonal Antibody HSF-2 Rat Monoclonal Antibody Hsp47 (Colligin) Monoclonal Antibody Hsp104 Polyclonal Antibody KDEL Antibody (Grp78, Grp94) Antibody KDEL Receptor Monoclonal Antibody Membrin Monoclonal Antibody p23 Polyclonal Antibody PDI Polyclonal Antibody PDI Monoclonal Antibody Sec6 Monoclonal Antibody TCP-1a Rat Monoclonal Antibody TCP-1a Rat Monoclonal Antibody TCP-1b Rat Monoclonal Antibody UGGT Polyclonal Antibody Hip Recombinant Protein HOP (p60) Recombinant Protein HSF-1 Recombinant Protein Hsp47 (Colligin) Recombinant Protein Active GrpE Recombinant Protein p23 Recombinant Protein HeLa Cell Lysate (Heat Shocked) Species H, M, R H, M, R, C, X H, M, R H M, R, B, C, X H, M, R, B H H, M, R, B H, B E. coli H, M, R, B H, M, R, B, C, X H, M, R, B H, M, R, B, C, D, X H, M, R, B H, M, R, B Y H, M, R, B, C, D, X H, M, R, B, C, D, X H, R, C H, M, R H, M, R, B, X H, M, R, B, C, X H, M, R, B, C M, R, B H, M, R, B, D, Y H, M, R, B, C M, R R H H H E. coli H Application WB WB, IP, ICC WB, IP, ICC, IHC WB, IP, ICC, IHC, F WB, IP, IHC WB WB, IP, IHC WB WB, IP, ICC, IHC WB, IP WB W,B IP WB, IP, ICC WB, IP, ICC WB, IP WB, IHC WB, IP WB, IP, ICC, IHC, F WB, IP, ICC WB, IP, ICC WB WB, IP, ICC WB, ICC, IHC WB, IP, ICC WB, IP, ICC WB, IP, F WB WB
16
Official Symbol AHSA1
Name AHA1, activator of Heat Shock 90kDa Protein ATPase homolog 1 (yeast) chaperone, ABC1 activity of bc1 complex homolog (S. pombe) Calreticulin
Synonyms AHA1, C14orf3, p38 ADCK3, COQ8
Entrez Gene ID 10598
Biological Function ATPase activity, Protein folding, Chaperone activity, Protein binding Kinase activity, Protein folding, Nucleotide binding DNA binding, Calcium homeostasis, Ion binding, Actin organization, Sugar binding, Protein export, Protein binding, Protein folding, Regulation of apoptosis, meiosis and transcription Ion binding, Angiogenesis, Sugar binding, Protein folding, Protein secretion Protein binding, Protein folding, CDK activity Endopeptidase activity, Proteolysis, Peptidase activity Ion binding, Protein folding, Nucleotide binding, Protein transport, Protein binding Exocytosis, Protein transport Isomerase activity, Protein folding, Protein binding
Tissue Distribution Broad
Cellular Distribution Cytoplasm, Endoplasmic Reticulum Mitochondrion
Human Diseases
CABC1
56997
CALR
RO, SSA, cC1qR
811
Broad
Cytoplasm Endoplasmic reticulum Extracellular environment Cytoplasm Endoplasmic reticulum Membrane Cytoplasm
CANX
Calnexin
CNX, IP90, P90
821
Broad
CDC37 ClpP
cell division cycle 37 homolog (S. cerevisiae) ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli) ClpX caseinolytic peptidase X homolog (E. coli) exocyst complex component 3 [Homo sapiens] FK506 binding protein 1A, 12kDa
P50CDC37
11140 8192
Broad
Mitochondrion
ClpX
10845
Broad
Mitochondrion
EXOC3 FKBP1A
SEC6, SEC6L1, Sec6p FKBP1; PKC12; PKCI2; FKBP12; PPIASE; FKBP-12; FKBP12C FKBP12.6, FKBP1L, FKBP9, OTK4, PKBP1L, PPIase FKBP51, FKBP54, P54, PPIase, Ptg-10 Bos1, GS27, Membrin
11336 2280
Plasma membrane Broad Cytoplasm, Sarcoplasmic Recticulum Cytoplasm Hypertension
FKBP1B
FK506 binding protein 1B, 12.6 kDa FK506 binding protein 5
2281
Isomerase activity, Muscle contraction, Protein folding FK506 binding, Protein folding, Isomerase activity, Protein binding Receptor activity, Vesicle mediated transport, Transporter activity, Protein transport DNA binding, Protein folding, Protein binding, Transcription, Transcriptional Activity DNA binding, Protein folding, Protein binding, Transcription, Transcriptional Activity DNA binding, Cell development, Transcriptional Activity, Cell proliferation, Protein folding, Transcription Nucleotide binding, Protein folding
Broadly
FKBP5
2289
Broad
Nucleus
Depression
GOSR2
Golgi SNAP receptor complex member 2
9570
Golgi apparatus, Endoplasmic reticulum, Membrane Broadly Cytoplasm, Nucleus Cytoplasm, Nucleus Nucleus
HSF1
Heat Shock transcription factor 1 Heat Shock transcription factor 2 Heat Shock transcription factor 4 Heat Shock 70kDa Protein 4-like Hsp70-interacting Protein KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1 [Homo sapiens] KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 2 [Homo s apiens] KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 3 [Homo sapiens] Protein disulfide isomerase family A, member 2
HSTF1
3297
HSF2
3298
Broadly
HSF4
CTM
3299
Broad
HSPA4L HSPBP1 KDELR1
APG-1, Osp94
22824 23640
Broad Broad
Cytoplasm, Nucleus
ERD2, ERD2.1, HDEL, PM23
10945
ER retention, Protein retention, Protein transport
Endoplasmic reticulum Golgi apparatus Endoplasmic reticulum Golgi apparatus Endoplasmic reticulum Membrane Endoplasmic reticulum
KDELR2
ELP-1; ERD2.2
11014
KDELR3
ERD2L3
11015
PDIA2
PDA2, PDI, PDIP, PDIR
64714
Isomerase activity, Apoptosis, Protein binding, Redox homeostasis, Protein folding, Protein retention
17
Chaperones & Others (continued)

Official Symbol PDIA3 Name Protein disulfide isomerase family A, member 3 Synonyms ERp57, ERp60, ERp61, GRP57, GRP58, P58, PI-PLC Entrez Gene ID 2923 Biological Function Cysteine endopeptidase activity, Redox homeostasis, Phospholipase C activity, Regulation of apoptosis, Protein binding, Protein import into nucleus, Disulfide isomerase activity, Protein retention in ER, Signal transuction Tissue Distribution Broad Cellular Distribution Endoplasmic reticulum Human Diseases
PDIA3P
Protein disulfide isomerase family A, member 3 pseudogene Protein disulfide isomerase family A, member 4 Protein disulfide isomerase family A, member 5 Protein disulfide isomerase family A, member 6 Prostaglandin E synthase 3 (cytosolic)
Erp60, GRP58P
171423
PDIA4
Erp70, Erp72
12304
Ion binding, Redox homeostasis, Isomerase activity, Protein secretion, Protein disulfide isomerase activity Isomerase activity, Electron transport, Oxidoreductase activity, Redox homeostasis, Protein folding Isomerase activity, Redox homeostasis, Protein folding Isomerase activity, Fatty acid biosynthesis, Prostaglandin E sytnhase, Prostanoid biosynthesis, Telomerase activity, Signal transduction, Telomere maintenance Binding, Response to stress, Protein folding Nucleotide binding, Protein folding Endopeptidase activity, Protein folding, Nucleotide binding Nucleotide binding, Protein folding Nucleotide binding, Protein folding Glucosyltransferase activity, Protein folding, Amino acid glysoylation Glucosyltransferase activity, Protein folding, Amino acid glysoylation Broad Broad Broad Broad
Endoplasmic reticulum Endoplasmic reticulum Endoplasmic reticulum Cytoplasm, Nucleus
PDIA5
FLJ30401, PDIR
10954
PDIA6 PTGES3
ERP5, P5, TXNDC7 P23, TEBP
10130 10728
STIP1
Stress-induced-phosphoprotein 1 (Hsp70/Hsp90organizing protein) t-complex 1 torsin family 1, member A (torsin A) torsin family 1, member B (torsin B) TNF receptor-associated Protein 1 UDP-glucose ceramide glucosyltransferase-like 1 UDP-glucose ceramide glucosyltransferase-like 2
HOP; P60; STI1L
10963
Golgi, Nucleus
TCP1 TOR1A
CCT-a, CCT1, CCTa, TCP-1-a DQ2, DYT1, torsin A DQ1 HSP75, HSP90L HUGT1 HUGT2
6950 1861
Cytoplasm Cytoplasmic,, Endoplasmic Reticulum Endoplasmic Reticulum Mitochondrion Endoplasmic reticulum Endoplasmic reticulum Dystonia
TOR1B TRAP1 UGCGL1 UGCGL2
27348 10131 56886 55757
Grp94 Monoclonal Antibody (Cat. No. SPA-850)

Human colon cancer CoCa-2 cells were analyzed by flow cytometry using isotype control antibody (left) or Grp94 monoclonal antibody (clone 9G10; right) at a final concentration of 10g/mL.
18
Grp75 Monoclonal Antibody (Cat. No. SPS-825)

Human breast cancer tissue was immunohistochemically stained using Grp75 monoclonal antibody (clone 30A5) at a dilution of 1:50.
TCP-1a Monoclonal Antibody (Cat. No. CTA-191)

Human colon cancer Coca-2 cells were analyzed by flow cytometry using isotype control antibody (left) or TCP-1a monoclonal antibody (clone 91a; right) at a final concentration of 10g/mL.
19
Hsp27 Review
expressed in a variety of tissues; their expression, however, is also up-regulated under conditions of stress as well as in a variety of disease settings14. Members of the sHSP family are categorized on the basis that they possess a conserved C-terminal region known as the a-crystallin domain and a variable N-terminal region. The a-crystallin domain consists of two anti-parallel b-sheets14. It is worth noting that while proteins like HSP32/HO-1 have also been categorized as sHSPs, they lack the critical C-terminal a-crystallin domain defining this family of heat shock proteins. The small heat shock family members vary in their respective molecular weights; they range in size from 15 kDa to 30 kDa. These proteins are known to exist as either homo- or heterocomplexes ranging in size from single units to large multimeric complexes up to approximately 700 kDa3. It is well documented that sHSP family members undergo post-translational modifications with the most common being the phosphorylation of serine residues. For instance, both the human form of aB-crystallin and HSP27 are phosphorylated on three serine residues. In the case of aB-crystallin, this protein is phosphorylated on Ser-19, Ser-45, and Ser-5913; whereas HSP27 is phosphorylated on Ser-15, Ser-78, and Ser-82, respectively16,22. While little homology exists in the sequences flanking these phosphorylation sites, there is definite overlap in regard to the kinases that phosphorylate these sites. In particular, the mitogen activated protein kinase activated protein kinase, MAPKAPK-2 is one of the key protein kinases able to phosphorylate many of these sites with the exception of Ser-19 on aB-crystallin, both in vitro and in vivo. At present, the kinase responsible for phosphorylating Ser-19 of on aB-crystallin has yet to be identified. Other kinases implicated in the phosphorylation of these serine sites are Erk-1 and Erk-2, which phosphorylate aBcrystallin15, and MAPKAPK-3, PKAca, p70S6K, PKD1, and PKCd, which phosphorylate HSP276,9,16,21,22.
HSP27: A regulator of cellular invasion. HSP27 localizes to focal adhesions, influences membrane dynamics and enhances the invasive phenotype of malignant cells.
Heat shock proteins (HSP), also known as molecular chaperones, are critical regulators of cellular homeostasis. Initially identified some forty years ago as heat responsive genes, HSPs have been reported to play important roles in the folding of nascent or new proteins, guiding the renaturation of misfolded or partly denatured proteins, as well as facilitating cellular turnover of client proteins8,12,14. In this regard, HSP90 and its associated co-chaperone complex is known to recruit E3 ubiquitin ligases under certain conditions, favoring the ubiquitinylation and degradation of the client proteins. However, in the presence of ATP, HSP90 complexes can favor the stabilization of these client proteins23. HSPs are categorized into six different families according to their respective molecular weights. They are the HSP100 family, the HSP90 family, the HSP70 family, the HSP60 family, the HSP40 family, and the small heat shock family (sHSPs) including HSP27.
Upstream Signals Leading to the Phosphorylation of HSP27

HSP27 has been reported to be phosphorylated in response to a variety of extracellular-derived signals including TNFa, thrombin, bFGF stimulation, as well as under conditions of heat shock and oxidative stress7,16. It is postulated that these pathways converge on and elicit their effects through p38 MAPK and MAPKAPK-2. p38 MAPK has been reported to phosphorylate MAPKAPK-2 in vitro on several residues including Thr-25, Thr-222, and Thr-334 leading to its activation5. Upon activation, MAPKAPK-2 is believed to phosphorylate HSP27 in
Small Heat Shock Family

The small heat shock family (sHSP) of molecular chaperones is a ubiquitously expressed group of proteins that is highly conserved among species. To date, ten sHSP isoforms have been identified and designated HSPB1 through HSPB10, respectively, with the most common being HSPB1 or HSP27, and HSPB5 or aB-crystallin14. Both HSP27 and aB-crystallin are constitutively
20
vivo. MAPKAPK-2, as well as MAPKAPK-3, has been reported to phosphorylate HSP27 in vitro on all three HSP27 phosphorylation sites, Ser-15, Ser-78, and Ser-8216,22. Studies utilizing the p38 inhibitor, SB203580, have also offered conclusive evidence that the p38 pathway is intimately involved in the post-translational regulation of HSP27. Treatment with SB203580, is able to attenuate the phosphorylation of HSP27 in response to various agonists18. More recently, both PKD1 and AKT1 have been ascribed as HSP27 phosphorylating kinases. PKD1 was shown to phosphorylate HSP27 in vitro, however, only on Ser-15 and Ser-829. AKT1, on the other hand, was shown to interact with p38 and phosphorylate HSP27 on Ser-8221.
HSP27: Clinical Ramifications

There is a wealth of evidence supporting the notion that heat shock proteins may contribute to the pathogenesis of human diseases like cancer, cardiovascular disease, and neurological disorders. Moreover, elevated expression of certain HSPs, like HSP27, has been reported to correlate with poor patient outcome in breast, ovarian, and prostate cancer8. This might, in part, be due to the effects HSP27 has on the cytoskeleton. Recently, HSP27 has been reported to behave as an actin-capping protein and influence actin dynamics; the latter of which was shown to be dependent upon the phosphorylation status of HSP274,17. In this regard, unphosphorylated monomeric HSP27 was shown to inhibit the polymerization of actin in vitro, whereas multimeric HSP27 complexes appeared to have no inherent effect on actin dynamics regardless of phosphorylation status. HSP27 has also been demonstrated to localize to focal adhesions, influence membrane dynamics, as well as influence invasive phenotype of cells2,11,24. More recently, HSP27 has been shown to play a role in the regulation of matrix metalloproteinase (MMP)-2 activity in prostate cancer cells24. Taken together, it would appear that disrupting the interactions between HSP27 and its binding partners, or reducing its expression in cancer might be a therapeutically valid approach when combined with conventional methodologies.
HSP27: Function
As a high molecular weight complex, HSP27 plays a critical role in the renaturation of misfolded or partly denatured proteins by specifically blocking their aggregation10. As with other phospho-proteins, this function is tightly linked with the phosphorylation status of HSP27. Phosphorylation of Ser-82 has been shown to result in HSP27 complex dissociation and the subsequent loss of its chaperoning activity. In addition to its chaperoning function, HSP27 has been shown to interact with different cytoskeletal elements affecting actin polymerization4 as well as inhibiting apoptosis7,19,20. Apoptosis, or programmed cell death, is a finely coordinated process involving the activation of a discrete network of enzymes, referred to as cellular caspases, that aid in preserving the fidelity of the human genome as well as turning over damaged or worn-out cells. While there is variation in terms of the mechanism by which apoptosis can be elicited (e.g., death receptor apoptosis vs. mitochondrial mediated apoptosis), these pathways converge on the key executioners of apoptosis, caspases-3, 6 and 7, to carry out the process. To counteract these pro-apoptotic mechanisms, the cell has devised a number of ways to inhibit this process. Two of the best-defined mechanisms involve the overexpression of the B-cell lymphoma protein, Bcl-2 and the activation of the anti-apoptotic kinase, AKT. More recently, HSP27 has also been ascribed as an anti-apoptotic protein. In particular, HSP27 has been reported to inhibit apoptosis (1) through its interactions with the death associated protein DAXX7, (2) by facilitating the activation of AKT21, and (3) by blocking the formation of the apoptosome19,20. Taken together, the overexpression of HSP27 in the context of a disease such as cancer, would facilitate adaptation to stressful conditions by aiding in the suppression of apoptosis, ultimately leading to a more aggressive phenotype. As such, it is not surprising that the overexpression of HSP27 correlates with poor patient prognosis in a variety of lesions.
HSP27: Phosphorylation linked to function. HSP27 is phosphorylated on key serine residues by MAPKAPK2 as well as MAPKAPK3 amongst others. Phosphorylation is associated with the dimerization of HSP27 and its function.
References on page 26
21
Hsp70 Review
Initially identified by Ritossa some forty years ago, heat shock proteins (HSP) were first identified as genes up-regulated in response to heat shock stimulation in Drosophila20. They are now recognized as proteins that play critical roles in cellular homeostasis and the adaptation to stressful conditions such as heat shock, oxidative stress, genotoxic shock, viral infection, and hypoxic conditions26. In part, the cytoprotective effects of HSPs are achieved through their role in the re-folding of partly denatured or misfolded proteins. HSPs are also known to be involved in: (1) the folding of newly formed proteins, (2) the trafficking of cellular proteins, as well as (3) the turn over of cellular proteins through the proteasomal pathway; as such, HSPs have been classified as molecular chaperones. HSPs are ubiquitously expressed and highly conserved among species, ranging from the simplest prokaryotes to complex eukaryotes such as humans. They are classified according to their respective molecular weights and are divided into six families: the small HSPs (sHSPs), the HSP40 family, the HSP60 family, the HSP70 family, the HSP90 family, and the HSP100 family. normal cellular function. Two other members of the HSP70 family under active investigation are the endoplasmic reticulum(ER) and mitochondrial-associated members, referred to as the glucose regulated proteins, GRP78 and GRP75. GRP78 plays a critical role in the ER-associated stress response, whereas GRP75 (also known as mortalin) is involved in the maintenance of mitochondrial function.
HSP70: Structure and Function

All HSP70 family members contain a highly conserved N-terminal ATPase domain of approximately 44 kDa which possesses weak ATPase activity under normal conditions. These proteins also contain an approximately 25 kDa C-terminal region which consists of a conserved hydrophobic peptide binding domain (PBD) of approximately 15 kDa, and a more variable a-helical domain of approximately 10 kDa5. The a-helical domain is classified as a cap believed to open and close in response to changes in the nucleotide binding status of HSP7015. The activity and function of HSP70 are thought to result from the binding of ATP to the N-terminus. In its ATP-bound state, the C-terminus of HSP70 is said to undergo a conformational change, resulting in the opening of the a-helical cap; this opening allows substrates to interact with the hydrophobic pocket of the PBD. In its ADP-bound state, it is believed that the a-helical cap is closed, excluding substrates from the PBD. Thus, in the presence of ATP, HSP70 is said to favor the folding of its client protein, as it has a lower affinity and faster processing rate than the ADP-bound form5,15. However, unlike other enzyme classes, members of the HSP70 family bind to a wide variety of client proteins through short hydrophobic segments found in unfolded, misfolded, or denatured proteins. On its own, members of the HSP70 family are known to possess little or no intrinsic ATPase activity. As with other heat shock proteins, ATPase activity and function are thought to be influenced through interactions with specific co-chaperone molecules. HSP70 co-chaperones include: (1) HSP40, which is believed to assist in loading targets on the HSP70 machinery3, (2) the HSC70 interacting protein, Hip, which binds to the ATPase domain stimulating its activity3, (3) the HSC70/HSP90 organizing protein, Hop, which serves as a link between HSP70 and HSP90 allowing for substrate exchange between the two chaperones, and also facilitates ATP/ADP cycling3, (4) the HSC70 unbinding protein, Hup, which facilitates the release of unfolded proteins3 , (5) the HSC70 accessory protein, Hap3, and the Bcl-2 associated athanogene proteins, BAG-1, BAG-2, and BAG-3, which interact with the ATPase domain and block the binding of unfolded proteins4,11,23,27, and (6) the carboxyl-terminus of HSP70 interacting protein, CHIP, which is believed to be a bona
The HSP70 Family

The HSP70 family represents one of the most widely examined heat shock families and consists of up to ten highly homologous members. Refer to Table 1 for a representative list of the HSP70 family members. As with other heat shock families, members of the HSP70 family differ in their spatial and subcellular distribution, as well as their expression levels under normal, unstressed conditions21,24. It is well established that the expression of some members of the HSP70 family can be induced under conditions of stress; as these proteins do not contain introns, they are able to be quickly up-regulated. While the expression of many HSP70 family members can be up-regulated in response to various stressors, the major stress inducible HSP70 members are the highly homologous genes HSP1A1 and HSPA1B, also referred to as HSP70-1 and HSP70-2, respectively. These proteins are expressed at relatively low or undetectable levels in most normal, unstressed cells; however, upon insult, their expression dramatically increases. It is worth noting, that HSPA6 and HSPA7, the two other highly related HSP70 inducible members known as HSP70B and HSP70B are up-regulated only under conditions of extreme stress21,24. At present, further research is required to elucidate the physiological importance of these two HSP70 family members. The constitutively expressed member of HSP70 family is HSPA8, also referred to as HSC70. HSC70 is ubiquitously expressed in all cell types and is believed to be responsible for maintaining
22
fide E3 ubiquitin ligase assisting in the ubiquitinylation of cellular proteins1,10,16. Overall, members of the HSP70 family are known to play critical roles in the folding of newly synthesized proteins; the re-folding of misfolded or denatured proteins; the trafficking of proteins across cellular membranes; the disassembly of clathrin-coated vesicles; the inhibition of protein aggregation; and the targeting and degradation of proteins via the proteasomal pathway3. More recently, HSP70 has also been demonstrated to suppress apoptosis in response to various stimuli12.
HSP70: Effects on Apoptosis

Apoptosis is a highly coordinated process that functions either through the activation of a discrete network of cysteine proteases known as cellular caspases, or through mechanisms not depending on caspase activation, known as caspase-independent cell death. The activation of cellular caspases can be achieved through various mechanisms including death signals provided at the level of the cell membrane, the mitochondria, and the endoplasmic reticulum. While these pathways rely on different initiators of apoptosis, they all converge on, and elicit their effects through, the executioner caspases mainly caspase-3, -6 and -7. Along with the activation of endonucleases, the activation of these caspases results in the dismantling of the cell and its intracellular contents, leading to the eventual formation of apoptotic bodies.
It is well established that the commitment to undergo apoptosis can be attenuated or blocked through various mechanisms, including the activation of key signal transduction molecules such as Akt, and the overexpression of certain cellular proteins such as Bcl-2. More recently, overexpression of heat shock proteins mainly members of the HSP70 family has also been demonstrated to inhibit apoptosis. Elevated expression of HSP70 has been reported to: (1) inhibit the formation of the apoptosome2, (2) inhibit the translocation of the Bcl-2 protein, Bax, to the mitochondrial membrane, ultimately blocking the release of cytochrome c from the mitochondria22, (3) inhibit the activation of cellular caspases19, (4) block the activation of the apoptosis signal regulating kinase, ASK118, (5) inhibit the activation of the stress kinase p388, and (6) inhibit JNK activation17.
HSP70: Clinical Ramifications in Cancer

There is a wealth of literature supporting the notion that heat shock proteins are elevated in a variety of human malignancies and that these increases in expression may not only contribute to the pathogenesis of the disease25, but may be of diagnostic, prognostic and therapeutic importance6. In this regard, HSP70 has been reported to correlate with poor differentiation in certain malignancies, increased lymph node metastases, chemo-resistance, and poor clinical outcome6,14. Further studies evaluating the importance of HSP70 family members in the initiation and progression of cancer will undoubtedly be of great clinical importance.
HSP70: A cell survival protein. HSP70 suppresses apoptosis by inhibiting the formation of the apoptosome and by blocking the activation of stress induced kinases including: ASK1, p38, and JNK, respectively.
References on page 26
23
Hsp90 Review
left: HSP90: A regulator of cell survival. Inhibition of HSP90 activity by drugs like geldanmycin destabilize client proteins which ultimately leads to the onset of apoptosis. right: HSP90: A drugable target. Inhibition of HSP90 by geldanmycin (GA) favors the ubiquitinylation and degradation of client proteins.
The heat shock, or stress family of proteins is a highly conserved, ubiquitously expressed class of proteins that have been demonstrated to be intimately involved in the regulation of cellular homeostasis in response to a myriad of environmental and physiological stressors27. The heat shock proteins (HSP) are classified into six different groups according to their respective molecular weights; they are the small heat shock proteins including HSP27, the HSP40 family, the HSP60 family, the HSP70 family, the HSP90 family, and the HSP100 family, respectively. HSPs, commonly referred to as molecular chaperones, were initially identified and described over thirty years ago as heat shock responsive genes. HSPs are now know to play critical roles in the stabilization of partly denatured or misfolded proteins, facilitate proper folding of nascent or new polypeptides as well as regulate the spatial distribution of cellular proteins. More recently, these molecular chaperones, mainly HSP90, have received significant attention for the putative roles they play in the pathogenesis and progression of human diseases like cancer21,35.
All members of the HSP90 family possess three specific domains: an N-terminal nucleotide binding pocket to which most clinical compounds are being developed6,22, a central domain important for ATPase activity11,19, and a C-terminal domain believed to act as a second nucleotide binding site9. HSP90 can either exist as a homodimer, a heterodimer, or as a multiprotein complex with other co-chaperones including HSP40, HSP70, Hop, and p2328. As with other heat shock families, dimerization is believed to be an ATP-dependent process. Unlike other member; however, the N-terminal nucleotide binding site of HSP90 is highly unique and bears a strong resemblance to members of the GKHL superfamily including bacterial gyrase, MutL and histidine kinases8. The mechanism(s) involved in regulating HSP90 activity and function, is at present unclear. However thought to involve: (1) post-translational modification including acetylation and phosphorylation1,17,20, (2) the N-terminal nucleotide binding status28, and (3) interactions with accessory co-chaperones28. Early studies evaluating the phosphorylation status of HSP90 revealed that phosphorylation of this target is essential for its activity. In this regard, HSP90 has been reported to be tyrosine phosphorylated in vivo when complexed with other proteins1. These specific phosphorylation sites have yet to be elucidated, however. More recently, the acetylation status of HSP90 has also been reported to influence the activity of HSP90. In particular, these studies revealed that hyperacetylation of HSP90 led to decrease in its association with the essential co-chaperone, p23, and a concomitant loss of chaperoning activity20. The specific acetylation sites have been yet to be reported. The N-terminal nucleotide binding status has also been demonstrated to influence the function of HSP90. In the presence of ATP and the appropriate upstream signals, HSP90 cyclizes with its co-chaperone molecules, stabilizing the expression of its client proteins. However, when bound by inhibitors like
HSP90: Structure and Function

The HSP90 family, which consists of both inducible and constitutive isoforms, is encoded at two distinct loci. Cellular homologues of the HSP90 family include: HSP90a (the inducible isoform), HSP90b (the constitutive isoform) Grp94 and Trap1, as well as the recently identified variant HSP90N. Whereas, HSP90a and HSP90b are predominantly cytosolic proteins and represent 1-2% of the normal cellular protein content, Grp94 and Trap1 are localized within the endoplasmic reticulum (ER) and mitochondria, respectively, and are expressed at much lower levels than their cytoplasmic counterparts28. HSP90N, on the other hand, preferentially localizes to the cellular membrane through its unique N-terminal hydrophobic region10.
24
Geldanamycin (GA), HSP90 function is impaired which results in the recruitment of E3 ubiquitin ligases favoring the ubiquitinylation and degradation of client proteins by the 26S proteasomal complex28. The stabilization versus degradation of proteins, in the presence of physiological stressors, may tip the balance in favor of stabilizing mutant proteins ultimately promoting an anti-apoptotic or pro-survival state. As with other heat shock proteins, HSP90 requires a number of co-chaperone molecules for its full function including HSP70, HSP40, Hip/Hop, p23, immunophilins, and CDC37/p5028. More recently, Aha1 (Activator of HSP90 ATPase homologue 1), which associates with the central domain of HSP90, was identified as a key molecular co-chaperone required for ATPase function18.
p53 has been marked as the master regulator of the human genome, knocking out this function of this essential protein through stabilization of the mutated form allows for the propagation of additional favorable oncogenic mutations, including those that facilitate progression of the disease e.g., invasion and metastasis.
HSP90: Clinical Ramifications in Cancer

Several lines of evidence support the notion that the expression levels of heat shock proteins are dramatically increased in a variety of human malignancies, both in solid and hematological types, and might contribute to the advancement of the disease3,5,7,12,15,16,21,23,24,26,34,35. As an example, elevated levels of HSP27 have been reported to correlate with poor patient outcome in prostate, breast, and ovarian cancer4. Moreover, compelling evidence suggests that HSP90, in the context of cancer, exists in a hyperactive state in the diseased tissue when compared with the normal surrounding material14. In its highly active state, the HSP90 complex would theoretically influence key signaling nexuses that would contribute to the pathogenesis of the disease; these include cell growth promotion, evasion of apoptosis, and stimulation of angiogenesis. In this regard, it has been postulated that changes in expression and activity levels are critical in that they provide a mechanism to counteract, or compensate, for the selective pressures these abnormal cells experience as the disease progresses including gene mutations, hypoxia, and growth pressures amongst others. As such, heat shock proteins, mainly HSP90, appear to provide a buffering mechanism facilitating the natural selection of the strongest cell lineage ultimately allowing for adaptation to the harshest of conditions. Consequently, based upon the uniqueness of the N-terminal nucleotide binding site, the differences in biological activity between the cancer and normal tissue, and the notion that HSP90 stabilizes key oncogenic client proteins, HSP90 has been suggested to serve as an excellent target for therapeutic intervention2,13,31. Not only is targeting HSP90 selecting against those adaptable cell lineages, but in addition, key oncogenic proteins would be destabilized and consequently degraded, shifting the balance towards an anti-proliferative pro-apoptotic state. Currently, there are on-going clinical trials evaluating the efficacy of these N-terminal specific inhibitors and a number of clinical candidates in the pipeline. Perhaps, the future will entail a combinatorial modality involving the administration of selective HSP90 inhibitors with conventional methodologies. References on page 26
HSP90: Client Proteins

In comparison to other members of the heat shock family, HSP90 client proteins are unique and tend to encompass key signal transduction molecules involved in the regulation of cellular growth, survival, and differentiation. In this regard, one of the first client proteins to be described was the transforming tyrosine kinase isolated from the Rous sarcoma virus, v-Src30,33. Since this original discovery, the number of client proteins influenced by HSP90 has significantly increased, many of which are linked with the pathogenesis of human cancer. Client proteins include serine/threonine and tyrosine kinases, transcription factors, and steroid receptors as well as certain tumor suppressor proteins. A concise list of clients influenced by HSP90 include: Akt/PKB, ASK1, Aurora B, Bcr-Abl, CDK1, CDK4, CHK1, CKII, ErbB2/Her-2, EGFR, ER, Hif-1a, c-Met, mutant p53, PLK, and Raf28. Two key signaling molecules influenced by HSP90, which are central to normal physiology, are the protein kinase Akt, and the tumor suppressor protein p53. In the case of Akt, HSP90 has been demonstrated to bind with the phosphorylated form and protect it from being inactivated by its dephosphorylating phosphatase, protein phosphatase (PP)-2A25. When active, Akt is known to provide anti-apoptotic signals, through various mechanisms, ultimately preventing the cells from undergoing apoptosis. In this regard, Akt in association with HSP90, has been demonstrated to phosphorylate and inhibit the apoptotic kinase ASK1, thus blocking apoptosis36. In the case of p53, HSP90 has been reported to bind with and stabilize the expression of the mutated form of this protein29. Stabilization of the mutated form provides a mechanism of knocking out the function of the normal wild-type p53 molecules through a dominant-negative effect. Functional p53 exists as a tetramer; as such, one mutated copy of p53 within this complex is capable of impairing normal p53 function. As
25
References
Hsp27 References
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CTA-123D CTA-123F CTA-191D CTA-191F CTA-202C CTA-202E EKS-500 EKS-600 EKS-650 EKS-700B EKS-725 EKS-750 EKS-800 EKS-810 EKS-895 ESP-502D ESP-502E ESP-540D ESP-540E ESP-555D ESP-555F ESP-581D ESP-581F ESP-715D ESP-715F ESP-741D ESP-741E HPK-101J HPK-102J LYC-HL101F NSP-510B NSP-510F NSP-535B NSP-535F NSP-540B NSP-540E NSP-550B NSP-550E NSP-555B NSP-555E OSA-110C OSA-110E OSA-111BC OSA-111BE OSA-111C OSA-111E OSA-111FIC OSA-111FIE OSA-150E OSA-200C OSA-200E SPA-110D SPA-110F SPA-210D SPA-210F
Product
Anti-TCP-1alpha (CCT), clone 23c (Rat IgG2c) Anti-TCP-1alpha (CCT), clone 23c (Rat IgG2c) Anti-TCP-1alpha (CCT), clone 91a (Rat IgG2a) Anti-TCP-1alpha (CCT), clone 91a (Rat IgG2a) Anti-TCP-1beta, clone PK/8/4/4i/2f Anti-TCP-1beta, clone PK/8/4/4i/2f Hsp27 StressXPress ELISA Kit HSP60 Antigen StressXPress ELISA Kit Anti-Human Hsp60 (total) StressXPress ELISA Kit Hsp70 StressXPress ELISA kit (B-version) Hsp70B StressXPress ELISA Kit Anti-Human Hsp70 (IgG/A/M) StressXPress ELISA Kit Heme Oxygenase-1 (HO-1), human, StressXPress ELISA Kit Heme Oxygenase-1 (HO-1), Rat StressXPress ELISA Kit Hsp90alpha StressXpress ELISA Kit Hsp70-A2 Protein - low Endotoxin Hsp70-A2 Protein - low Endotoxin Hsp60 Protein - low Endotoxin Hsp60 Protein - low Endotoxin Hsp70 (Hsp72) Protein - low Endotoxin Hsp70 (Hsp72) Protein - low Endotoxin Hsp65 Protein - low Endotoxin Hsp65 Protein - low Endotoxin Hsp27 - low Endotoxin Hsp27 - low Endotoxin Hsp60 (Mouse) - low Endotoxin Hsp60 (Mouse) - low Endotoxin 17-AAG Geldanamycin HeLa Cell Lysate, Heat Shocked Hsp25 Protein Hsp25 Protein Hsp47 (Colligin) Protein Hsp47 (Colligin) Protein Hsp60 Protein Hsp60 Protein HO-2 (Heme Oxygenase-2) Protein HO-2 (Heme Oxygenase-2) Protein HSP70 (Hsp72) Protein HSP70 (Hsp72) Protein Anti-HO-1, clone HO-1-1 Anti-HO-1, clone HO-1-1 Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, Biotin Conjugate Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, Biotin Conjugate Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2 Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2 Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, FITC conjugated Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, FITC conjugated Anti-HO-1 (Heme Oxygenase-1, Hsp32) Anti-HO-2 (Heme Oxygenase-2) Anti-HO-2 (Heme Oxygenase-2) Anti-Cpn10 Anti-Cpn10 Anti-GroES Anti-GroES
Size
50 200 50 200 25 100 1 1 1 1 1 1 1 1 1 50 100 50 100 50 200 50 200 50 200 50 100 1 1 200 20 200 20 200 20 100 20 100 20 100 25 100 25 100 25 100 25 100 100 25 100 50 200 50 200 g g g g g g kit kit kit kit kit kit kit kit kit g g g g g g g g g g g g mg mg g g g g g g g g g g g g g g g g g g g l l l l l l l
Price E
175 372 175 372 175 372 753 753 753 890 897 753 753 753 864 415 599 415 599 415 1109 416 1111 415 1100 415 599 339 193 110 179 479 148 390 221 479 207 421 179 479 211 430 220 464 207 450 233 479 532 266 532 218 434 169 372
Your antibody reference: www.antibodyworld.com
CONTACT US TODAY BIOMOL GmbH Waidmannstr. 35 22769 Hamburg Germany info@biomol.de www.biomol.de Phone: +49 (0)40-853 260 0 Fax: +49 (0)40-853 260 22 TOLL FREE IN GERMANY Phone: 0800-246 66 51 Fax: 0800-246 66 52

Price List
Cat. No.
SPA-221D SPA-221F SPA-222D SPA-222F SPA-223D SPA-223F SPA-224D SPA-224F SPA-225C SPA-225E SPA-226C SPA-226E SPA-227C SPA-227E SPA-230D SPA-230F SPA-240D SPA-240F SPA-400C SPA-400E SPA-410D SPA-410F SPA-450E SPA-470D SPA-470F SPA-523D SPA-523F SPA-523PUC SPA-523PUE SPA-524D SPA-524F SPA-524PUC SPA-524PUE SPA-525C SPA-525E SPA-585C SPA-585E SPA-600D SPA-600F SPA-601D SPA-601F SPA-670C SPA-670E SPA-725C SPA-725E SPA-754E SPA-756D SPA-757C SPA-757E SPA-766C SPA-766E SPA-796E SPA-800BD SPA-800BF SPA-800FID SPA-800FIF SPA-801E SPA-803D SPA-803F SPA-806D SPA-806F SPA-807D SPA-807F SPA-810APD SPA-810APF SPA-810BD SPA-810BF SPA-810D
Product
Anti-alpha A Crystallin Anti-alpha A Crystallin Anti-alpha B Crystallin, clone 1B6.1-3G4 Anti-alpha B Crystallin, clone 1B6.1-3G4 Anti-alpha B Crystallin Anti-alpha B Crystallin Anti-alpha A/alpha B-Crystallin Anti-alpha A/alpha B-Crystallin Anti-phospho-Crystallin, alphaB (Ser19) Anti-phospho-Crystallin, alphaB (Ser19) Anti-phospho-Crystallin, alphaB (Ser45) Anti-phospho-Crystallin, alphaB (Ser45) Anti-phospho-Crystallin, alphaB (Ser59) Anti-phospho-Crystallin, alphaB (Ser59) Anti-beta-Crystallin, clone 3.H9.2 Anti-beta-Crystallin, clone 3.H9.2 Anti-GrpE Anti-GrpE Anti-Hsp40 (Heat Shock Protein 40, HDJ1) Anti-Hsp40 (Heat Shock Protein 40, HDJ1) Anti-DnaJ Anti-DnaJ Anti-Hsp40 (Heat Shock Protein 40, HDJ1), clone 2E1 Anti-Hsp47 (Colligin), clone M16.10A1 Anti-Hsp47 (Colligin), clone M16.10A1 Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser82) Anti-phospho-Hsp27 (Ser82) Anti-phospho-Hsp27 (Ser82) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser82) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser15) (Heat Shock Protein 27) Anti-phospho-Hsp27 (Ser15) (Heat Shock Protein 27) Anti-ERp57 (Grp58) Anti-ERp57 (Grp58) Anti-Calreticulin Anti-Calreticulin Anti-Calreticulin, clone FMC75 Anti-Calreticulin, clone FMC75 Anti-p23 Anti-p23 Anti-Erp57, clone MaP.Erp57 Anti-Erp57, clone MaP.Erp57 Anti-Hsp70B (Heat Shock Protein 70B), clone 165f Anti-Hsp70B (Heat Shock Protein 70B) Anti-Hsp70, Hsc70 (Heat Shock Protein 70, Heat Shock Cognate Protein 70) Anti-Hsp70, Hsc70 (Heat Shock Protein 70, Heat Shock Cognate Protein 70) Anti-Hip Anti-Hip Anti-Hsp20 (Heat Shock Protein 20) Anti-Hsp27 (Heat Shock Protein 27), Biotin conjugate, clone G3.1 Anti-Hsp27 (Heat Shock Protein 27), Biotin conjugate, clone G3.1 Anti-Hsp27 (Heat Shock Protein 27), clone G3.1, FITC conjugated Anti-Hsp27 (Heat Shock Protein 27), clone G3.1, FITC conjugated Anti-Hsp25 (Heat Shock Protein 25) Anti-Hsp27 (Heat Shock Protein 27) Anti-Hsp27 (Heat Shock Protein 27) Anti-Hsp60 (Heat Shock Protein 65), clone LK-1 Anti-Hsp60 (Heat Shock Protein 65), clone LK-1 Anti-Hsp60 (Heat Shock Protein 65), clone LK-2 Anti-Hsp60 (Heat Shock Protein 65), clone LK-2 Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, AP-conjugated Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, AP-conjugated Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, Biotin-conjugated Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, Biotin-conjugated Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5
Size
50 200 50 200 50 200 50 200 25 100 25 100 25 100 50 200 50 200 25 100 50 200 100 50 200 50 200 25 100 50 200 25 100 25 100 25 100 50 200 50 200 25 100 25 100 100 50 25 100 25 100 100 50 200 50 200 100 50 200 50 200 50 200 50 200 50 200 50 l l g g l l l l g g g g g g g g l l l l l l g g g l l l l l l l l g g l l l l g g l l g g g l l l l l g g g g g l l l g g g g l l g g g
Price E
173 365 175 372 173 365 160 355 154 345 154 345 154 345 175 372 173 365 199 421 188 428 368 207 450 207 421 170 375 199 409 170 375 207 421 150 338 161 355 182 399 140 318 150 338 451 464 148 299 148 331 344 187 395 187 395 355 161 355 160 356 182 394 228 470 220 463 207
BIOMOL GmbH Bestellen in Deutschland Fon: 0800-2 46 66 51 Fax: 0800-2 46 66 52 info@biomol.de www.biomol.de Technischer Support: ts@biomol.de Cat. No.
SPA-810F SPA-810FIE SPA-810FIH SPA-811D SPA-811F SPA-812C SPA-812E SPA-815APD SPA-815APF SPA-815D SPA-815F SPA-816D SPA-816F SPA-820APD SPA-820APF SPA-820D SPA-820F SPA-822D SPA-822F SPA-826D SPA-826F SPA-827D SPA-827F SPA-828C SPA-828E SPA-829C SPA-829E SPA-830D SPA-830F SPA-835D SPA-835F SPA-840D SPA-840F SPA-842C SPA-842E SPA-843C SPA-843E SPA-845D SPA-845F SPA-846C SPA-846E SPA-860D SPA-860F SPA-865D SPA-865F SPA-890D SPA-890F SPA-891D SPA-891F SPA-895D SPA-895F SPA-896C SPA-896E SPA-897E SPA-901D SPA-901F SPA-950C SPA-950E SPA-960C SPA-960E SPA-1040D SPA-1040F SPA-1101D SPA-1101F SPA-1103D SPA-1103F SPP-225J SPP-225L
Product
Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5 Anti-Hsp70 (Heat Shock Protein 70), clone C92F3A-5, FITC conjugated Anti-Hsp70 (Heat Shock Protein 70), clone C92F3A-5, FITC conjugated Anti-Hsp70 (Heat Shock Protein, Hsp72) Anti-Hsp70 (Heat Shock Protein, Hsp72) Anti-Hsp70 (Heat Shock Protein, Hsp72) Anti-Hsp70 (Heat Shock Protein, Hsp72) Anti-Hsc70 (Hsp73), clone 1B5 (Rat), AP-conjugated Anti-Hsc70 (Hsp73), clone 1B5 (Rat), AP-conjugated Anti-Hsc70 (Hsp73), clone 1B5 (Rat) Anti-Hsc70 (Hsp73), clone 1B5 (Rat) Anti-Hsc70 (Hsp73) Anti-Hsc70 (Hsp73) Anti-Hsp70/Hsc70, AP conjugate Anti-Hsp70/Hsc70, AP conjugate Anti-Hsp70/Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone N27F3-4 Anti-Hsp70/Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone N27F3-4 Anti-Hsp70, Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone BB70 Anti-Hsp70, Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone BB70 Anti-Grp78 (BiP) Anti-Grp78 (BiP) Anti-KDEL, clone 10C3 Anti-KDEL, clone 10C3 Anti-Hsp60 (Heat Shock Protein 60) Anti-Hsp60 (Heat Shock Protein 60) Anti-Hsp60 (Heat Shock Protein 65), clone Mab-11-13 Anti-Hsp60 (Heat Shock Protein 65), clone Mab-11-13 Anti-Hsp90 (Heat Shock Protein 90), clone AC88 Anti-Hsp90 (Heat Shock Protein 90), clone AC88 Anti-Hsp90 (Heat Shock Protein 90), clone 16F1 Anti-Hsp90 (Heat Shock Protein 90), clone 16F1 Anti-Hsp90 alpha, clone 9D2 Anti-Hsp90 alpha, clone 9D2 Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3705 Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3705 Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3701 Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3701 Anti-Hsp90 (Heat Shock Protein 90), clone 2D12 Anti-Hsp90 (Heat Shock Protein 90), clone 2D12 Anti-Hsp90 (Heat Shock Protein 90) Anti-Hsp90 (Heat Shock Protein 90) Anti-Calnexin-C Anti-Calnexin-C Anti-Calnexin Anti-Calnexin Anti-PDI (Protein Disulfide Isomerase) Anti-PDI (Protein Disulfide Isomerase) Anti-PDI (Protein Disulfide Isomerase), clone 1D3 Anti-PDI (Protein Disulfide Isomerase), clone 1D3 Anti-HO-1 (Hsp32, Heme Oxygenase-1) Anti-HO-1 (Hsp32, Heme Oxygenase-1) Anti-HO-1 (Hsp32, Heme Oxygenase-1) Anti-HO-1 (Hsp32, Heme Oxygenase-1) Anti-HO-2 (Heme Oxygenase-2) Anti-HSF-1 Anti-HSF-1 Anti-HSF-1, clone 10H8 (Rat) Anti-HSF-1, clone 10H8 (Rat) Anti-HSF-2, Rat monoclonal IgG 3F2 Anti-HSF-2, Rat monoclonal IgG 3F2 Anti-Hsp104 (Heat Shock Protein 104) Anti-Hsp104 (Heat Shock Protein 104) Anti-Hsp110/70 (Family) Anti-Hsp110/70 (Family) Anti-Hsp104 (Heat Shock Protein 104) Anti-Hsp104 (Heat Shock Protein 104) Crystallin, alpha Crystallin, alpha
Size
200 100 400 50 200 25 100 50 200 50 200 50 200 50 200 50 200 50 200 50 200 50 200 25 100 100 50 200 50 200 50 200 25 100 25 100 50 200 25 100 50 200 50 200 50 200 50 200 50 200 25 100 100 50 200 25 100 25 100 50 200 50 200 50 200 1 5
Price E
g 450 g 228 g 470 l 211 l 421 l 211 l 421 l 212 l 493 g 207 g 479 l 212 l 378 l 212 l 493 g 207 g 450 g 207 g 450 l 207 l 450 g 207 g 421 l 144 l 293 discontinued l 356 g 207 g 450 g 190 g 421 g 161 g 355 g 144 g 322 g 144 g 322 l 161 l 355 l 144 l 293 l 215 l 472 l 215 l 472 l 194 l 430 g 194 g 430 l 179 l 394 l 161 l 355 g 434 l 214 l 434 g 147 g 327 g 147 g 327 l 175 l 372 l 174 l 386 l 174 l 386 mg 48 mg 183

Price List
Cat. No.
SPP-226B SPP-226F SPP-227B SPP-227F SPP-400B SPP-400E SPP-610C SPP-610G SPP-620C SPP-620E SPP-620F SPP-640D SPP-640F SPP-650C SPP-650E SPP-650F SPP-715F SPP-730D SPP-730F SPP-732B SPP-732E SPP-741B SPP-741D SPP-741F SPP-742B SPP-742E SPP-751D SPP-751F SPP-752B SPP-752E SPP-758B SPP-758E SPP-762B SPP-762E SPP-765B SPP-765E SPP-767E SPP-770B SPP-770E SPP-776D SPP-776F SPP-900B SPP-900E SPS-771D SPS-771F SPS-825D SPS-870D SPS-870F SPS-875D SPS-875F SRA-1400D SRA-1400F SRA-1500D SRA-1500F SRP-1510B SRP-1510E VAA-PT048C VAA-PT048E VAM-PT046C VAM-PT046E VAM-SV021C VAM-SV021E VAP-PT068C VAP-PT068E VAP-SV003D
Product
Crystallin, alphaA Crystallin, alphaA Crystallin, alphaB Crystallin, alphaB Hsp40 Protein Hsp40 Protein GroEL Protein GroEL Protein GroES Protein GroES Protein GroES Protein DnaJ Protein DnaJ Protein GrpE Protein GrpE Protein GrpE Protein Hsp27 Protein HO-1 (Hsp32, Heme Oxygenase-1) HO-1 (Hsp32, Heme Oxygenase-1) HO-1 (Hsp32, Heme Oxygenase-1) Protein HO-1 (Hsp32, Heme Oxygenase-1) Protein Hsp60 Protein Hsp60 Protein Hsp60 Protein Hsp60 Protein Hsp60 Protein Hsc70 (Hsp73) Active Protein Hsc70 (Hsp73) Active Protein Hsc70 (Hsp73) Protein-ATPase Fragment Hsc70 (Hsp73) Protein-ATPase Fragment Hsp70 Protein, rat Hsp70 Protein, rat Hsp70B Protein Hsp70B Protein Grp78 (BiP) Protein Grp78 (BiP) Protein Hip Protein Hsp90 Protein Hsp90 Protein Hsp90 alpha Protein Hsp90 alpha Protein HSF-1 Protein HSF-1 Protein Anti-Hsp90 alpha Anti-Hsp90 alpha Anti-Grp75, clone 30A5 Anti-GroEL, clone 9A1/2 Anti-GroEL, clone 9A1/2 Anti-GroEL Anti-GroEL Anti-FKBP59 (Hsp56, p59), clone KN382/EC1 Anti-FKBP59 (Hsp56, p59), clone KN382/EC1 Anti-Hop (p60), clone DS14F5 Anti-Hop (p60), clone DS14F5 HOP (p60) Protein HOP (p60) Protein Anti-KDEL Receptor, clone KR-10 Anti-KDEL Receptor, clone KR-10 Anti-Membrin, clone 4HAD6 Anti-Membrin, clone 4HAD6 Anti-rSec6, clone 9H5 Anti-rSec6, clone 9H5 Anti-UGGT Anti-UGGT Anti-Cysteine String Protein (CSP)
Size
20 200 20 200 20 100 25 250 25 100 200 50 200 25 100 200 200 50 200 20 100 20 50 200 20 100 50 200 20 100 20 100 20 100 20 100 100 20 100 50 200 20 100 50 200 50 50 200 50 200 50 200 50 200 20 100 25 100 25 100 25 100 25 100 50 g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g g l l l l l l l g g g g g g l l g g g g l l g
Price E
114 356 114 356 207 450 144 208 148 287 434 499 1272 148 217 364 479 349 799 212 434 228 299 887 221 479 254 699 144 355 228 492 179 479 136 378 421 177 432 179 421 212 434 161 355 421 156 348 175 396 228 399 173 365 199 409 199 390 173 365 160 355 173 365 372
Your antibody reference: www.antibodyworld.com
CONTACT US TODAY BIOMOL GmbH Waidmannstr. 35 22769 Hamburg Germany info@biomol.de www.biomol.de Phone: +49 (0)40-853 260 0 Fax: +49 (0)40-853 260 22 TOLL FREE IN GERMANY Phone: 0800-246 66 51 Fax: 0800-246 66 52
Alle Preise zzgl. MwSt. und Versandkosten. Preisnderungen und Irrtmer vorbehalten. 06/2007

HSP Proteins

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HSP Proteins

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Heat Shock Proteins and Molecular Chaperones

Hsp10 Hsp27 Hsp32 Hsp40 Hsp60 Hsp70 Hsp90 Hsp110 Chaperones

Heat Shock Proteins and Molecular Chaperones

Bei Biomol erhalten Sie die Assay Design- und Stressgen-Produkte:

Assay Designs (Stressgen) Products

Hsp27 Review on page 20

WB, IP WB, ICC, IHC WB, IP WB WB, IP WB, IP WB, IP WB

Heat Shock 27kDa Protein 1

Charcot-MarieTooth disease, axonal, type 2F. Neuropathy, distal hereditary motor

HSPB2 HSPB3 HSPB6

MKBP HSPL27 Hsp20

3316 8988 126393

Heart, Skeletal Muscle, Skin Muscle Muscle, Ovary

Actin cytoskeleton Contractile Fibers

Cardiac, Connective, Skeletal Broadly

H11; E2IG1; HSP22

Kinase Activity, Transferase Activity, Protein Folding

Cytoplasm, Plasma Membrane

CharcotMarie-Tooth disease type 2L. Hereditary motor neuropathy type II

Nucleus, Cytoplasm Cytoplasm

Structural activity, Cell differentiation, Spermatogenesis

Hsp27 (phospho-Ser82) Polyclonal Antibody (Cat. No. SPA-524)

H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast

Hsp32 (Heme Qxygenase)

Heme-Oxygenase-1 (Hsp32) Monoclonal Antibody (Cat. No. OSA-111)

Heme Oxygenase 1 (Hsp32)

Heme-Oxygenase-1 (Hsp32) Monoclonal Antibody (Cat. No. OSA-110)

Hsp40 and the DnaJ Family

CPR3; DJA2; DNAJ; DNJ3; RDJ2; HIRIP4 TID1, hTid-1

Cytoplasm Endoplasmic reticulum Nucleolus Nucleus Cytoplasm Endoplasmic reticulum Nucleus

DnaJ (Hsp40) homolog, subfamily B, member 11

EDJ; ERj3; HEDJ; hDj9; ABBP2; ERdj3; ABBP-2

Protein binding, Protein folding

datasheet: www.biomol.de www.antibodyworld.com

Zrf1; Zrf2; MIDA1

DNAJC3 DNAJC4 DNAJC5 DNAJC5B DNAJC5G DNAJC6

5611 3338 80331 85479 285126 9829

Cytoplasm Membrane Membrane

TPR2; TTC2; DANJC7 SPF31; HSPC331 JDD1; SB73 JPDI; ERdj5

7266 22826 23234 54431 55735

Endoplasmic Reticulum Mitochondrion

JDP1 RME8 DNAJ; HDJ3; LIP6 MCJ; HSD18; DNAJD1

56521 23317 85406 29103 23341 55192 202052

Endosome Endoplasmic reticulum

Membrane Membrane Mitochondrion Mitochondrion

TIM14; TIMM14 HSCB, JAC1; HSC20

H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast

Hsp47 Monoclonal Antibody (Cat. No. SPA-470)

Hsp60 and GroEL: the Chaperonins

Assay Designs (Stressgen) Products

Hsp60 Monoclonal Antibody (Cat. No. SPA-807)

Hsp60 Monoclonal Antibody (Cat. No. SPA-829)

Hsp60 Monoclonal Antibody (Cat. No. SPA-806)

Hsp70 and DnaK

Hsp70 Review on page 22

Assay Designs (Stressgen) Products

datasheet: www.biomol.de www.antibodyworld.com

Heat Shock 70kDa Protein 1B

Nucleotide binding, Protien folding, Regulation of apoptosis

Cytoplasm, Endoplasmic reticulum, Mitochondrion Nucleus Cytoplasm, Nucleus

Heat Shock 70kDa Protein 1-like

Nucleotide binding, DNA repair, Protein folding, Telomere maintenance