SDS-PAGE 1

SDS-PAGE
SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel
electrophoresis, is a technique widely used in
biochemistry, forensics, genetics and molecular biology to
separate proteins according to their electrophoretic mobility
(a function of length of polypeptide chain or molecular
weight). SDS gel electrophoresis of samples having
identical charge per unit mass due to binding of SDS results
in fractionation by size.

Procedure

Tissue preparation
Samples may be taken from whole tissue or from cell
culture. In most cases, solid tissues are first broken down
mechanically using a blender (for larger sample volumes),
using a homogenizer (smaller volumes), or by sonication. Picture of an SDS-PAGE. The molecular marker is in the left
Cells may also be broken open by one of the above lane
mechanical methods. However, it should be noted that
bacteria, virus or environmental samples can be the source of protein and thus Western blotting is not restricted to
cellular studies only.

A combination of biochemical and mechanical techniques – including various types of filtration and centrifugation –
can be used to separate different cell compartments and organelles.
The solution of proteins to be analyzed is mixed with SDS, an anionic detergent which denatures secondary and
non–disulfide–linked tertiary structures, and applies a negative charge to each protein in proportion to its mass.
Heating the samples to at least 60 degrees C shakes up the molecules, helping SDS to bind. [1] [2] [3] [4]
A tracking dye may be added to the protein solution (of a size smaller than protein) to allow the experimenter to
track the progress of the protein solution through the gel during the electrophoretic run.
SDS-PAGE 2

Preparing acrylamide gels

The gels generally consist of acrylamide, bisacrylamide, SDS, and a Tris-Cl buffer with adjusted pH. The solution is
degassed under a vacuum to prevent air bubbles during polymerization. [5] Ammonium persulfate and TEMED are
added when the gel is ready to be polymerized. The separating or resolving gel is usually more basic and has a
higher polyacrylamide content than the loading gel. [6]

Gels are polymerized in a gel caster. First the separating gel is poured and allowed to polymerize. Next a thin layer
of isopropanol is added. Next the loading gel is poured and a comb is placed to create the wells. After the loading gel
is polymerized the comb can be removed and the gel is ready for electrophoresis.
SDS-PAGE 3

Electrophoresis
First the anode and cathode buffers are prepared. The anode buffer usually contains Tris-Cl, distilled deionized water
and is adjusted to a higher pH than the cathode buffer. The cathode buffer contains SDS, Tris, Tricine, and distilled
deionized water. [7] [8]

The electrophoresis apparatus is set up with cathode buffer covering the gel in the negative electrode chamber, and
anode buffer in the lower positive electrode chamber. Next, the denatured sample proteins are added to the wells one
end of the gel with a syringe or pipette. Finally, the apparatus is hooked up to a power source under appropriate
running conditions to separate the protein bands.

An electric field is applied across the gel, causing the negatively-charged proteins to migrate across the gel towards
the positive (+) electrode (anode). Depending on their size, each protein will move differently through the gel matrix:
short proteins will more easily fit through the pores in the gel, while larger ones will have more difficulty (they
encounter more resistance). After a set amount of time (usually a few hours- though this depends on the voltage
applied across the gel; higher voltages run faster but tend to produce somewhat poorer resolution), the proteins will
have differentially migrated based on their size; smaller proteins will have traveled farther down the gel, while larger
ones will have remained closer to the point of origin. Therefore, proteins may be separated roughly according to size
(and therefore, molecular weight), certain glycoproteins behave anomalously on SDS gels.
SDS-PAGE 4

Staining
Following electrophoresis, the gel may be stained (most commonly
with Coomassie Brilliant Blue R-250 or silver stain), allowing
visualization of the separated proteins, or processed further (e.g.
Western blot). After staining, different proteins will appear as distinct
bands within the gel. It is common to run molecular markers of known
molecular weight in a separate lane in the gel, in order to calibrate the
gel and determine the weight of unknown proteins by comparing the
distance traveled relative to the marker. The gel is actually formed
because the acrylamide solution contains a small amount, generally
Two SDS-PAGE-gels after a completed run
about 1 part in 35 of bisacrylamide, which can form cross-links
between two polyacrylamide molecules. The ratio of acrylamide to
bisacrylamide can be varied for special purposes. The acrylamide concentration of the gel can also be varied,
generally in the range from 5% to 25%. Lower percentage gels are better for resolving very high molecular weight
proteins, while much higher percentages are needed to resolve smaller proteins. Determining how much of the
various solutions to mix together to make gels of particular acrylamide concentration can be done on line [9]

Gel electrophoresis is usually the first choice as an assay of protein purity due to its reliability and ease. The
presence of SDS and the denaturing step causes proteins to be separated solely based on size. False negatives and
positives are possible. A comigrating contaminant can appear as the same band as the desired protein. This
comigration could also cause a protein to run at a different position or to not be able to penetrate the gel. This is why
it is important to stain the entire gel including the stacking section. Coomassie Brilliant Blue will also bind with less
affinity to glycoproteins and fibrous proteins, which interferes with quantification.

Chemical ingredients and their roles

Polyacrylamide gel (PAG) had been known as a potential embedding medium for sectioning tissues as early as 1964.
Two independent groups, Davis and Raymond, employed PAG in electrophoresis in 1959.[10] [11] It possesses
several electrophoretically desirable features that make it a versatile medium. PAGE separates protein molecules
according to both size and charge. It is a synthetic gel, thermo-stable, transparent, strong, relatively chemically inert,
can be prepared with a wide range of average pore sizes [12] . The pore size of a gel is determined by two factors, the
total amount of acrylamide present (%T) (T = Total acrylamide-bisacrylamide monomer concentration) and the
amount of cross-linker (%C) (C = Crosslinker concentration). Pore size decreases with increasing %T; with
cross-linking, 5%C gives the smallest pore size. Any increase or decrease in %C increases the pore size, as pore size
with respect to %C is a parabolic function with vertex as 5%C. This appears to be because of nonhomogeneous
bundling of strands in the gel.
This gel material can also withstand high voltage gradients, feasible for various staining and destaining procedures,
and can be digested to extract separated fractions or dried for autoradiography and permanent recording. DISC
electrophoresis utilizes gels of different pore sizes. [13] [14] The name DISC was derived from the discontinuities in
the electrophoretic matrix and coincidentally from the discoid shape of the separated zones of ions. There are two
layers of gel, namely stacking or spacer gel, and resolving or separating gel.
SDS-PAGE 5

Stacking gel
The stacking gel is a large pore PAG (4%T). This gel is
prepared with Tris/HCl buffer pH 6.8 of about 2 pH
units lower than that of electrophoresis buffer
(Tris/Glycine). These conditions provide an
environment for Kohlrausch reactions determining
molar conductivity, as a result, SDS-coated proteins are
concentrated to several fold and a thin starting zone of
the order of 19 μm is achieved in a few minutes. This
gel is cast over the resolving gel. The height of the
stacking gel region is always maintained more than
double the height and the volume of the sample to be
applied. This is based on isotachophoresis.

Chemical ingredients
• Tris (tris (hydroxy methyl) aminomethane)
(C4H11NO3; mW: 121.14). It has been used as a
buffer because it is an innocuous substance to most
proteins. Its pKa is 8.3 at 20 °C, making it a very
Transmission-Electron Microscopic image of a polyacrylamide gel.
satisfactory buffer in the pH range from roughly 7 to The pore size of a gel is determined by the total amount of monomer
9. present (%T) and the amount of cross-linker (%C).

• Glycine (Amino Acetic Acid) (C2H5NO2; mW:

75.07). Glycine has been used as the source of trailing ion or slow ion because its pKa is 9.69 and mobility of
glycinate are such that the effective mobility can be set at a value below that of the slowest known proteins of net
negative charge in the pH range. The minimum pH of this range is approximately 8.0.
• Acrylamide (C3H5NO; mW: 71.08). It is a white crystalline powder. While dissolving in water,
autopolymerization of acrylamide takes place. It is a slow spontaneous process by which acrylamide molecules
join together by head on tail fashion. But in presence of free radicals generating system, acrylamide monomers
are activated into a free-radical state. These activated monomers polymerise quickly and form long chain
polymers. This kind of reaction is known as Vinyl addition polymerisation. A solution of these polymer chains
becomes viscous but does not form a gel, because the chains simply slide over one another. Gel formation
requires hooking various chains together. Acrylamide is a neurotoxin. It is also essential to store acrylamide in a
cool dark and dry place to reduce autopolymerisation and hydrolysis.
• Bisacrylamide (N,N'-Methylenebisacrylamide) (C7H10N2O2; mW: 154.17). Bisacrylamide is the most
frequently used cross linking agent for poly acrylamide gels. Chemically it is thought of having two-acrylamide
molecules coupled head to head at their non-reactive ends.
• Sodium Dodecyl Sulfate (SDS) (C12H25NaO4S; mW: 288.38). SDS is the most common dissociating agent
used to denature native proteins to individual polypeptides. When a protein mixture is heated to 100 °C in
presence of SDS, the detergent wraps around the polypeptide backbone. It binds to polypeptides in a constant
weight ratio of 1.4 g/g of polypeptide. In this process, the intrinsic charges of polypeptides becomes negligible
when compared to the negative charges contributed by SDS. Thus polypeptides after treatment becomes a rod like
structure possessing a uniform charge density, that is same net negative charge per unit length. Mobilities of these
proteins will be a linear function of the logarithms of their molecular weights.
Without SDS, different proteins with similar molecular weights would migrate differently due to differences in
mass charge ratio, as each protein has an isoelectric point and molecular weight particular to its primary
SDS-PAGE 6

structure. This is known as Native PAGE. Adding SDS solves this problem, as it binds to and unfolds the
protein, giving a near uniform negative charge along the length of the polypeptide.
• Ammonium persulfate (APS) (N2H8S2O8; mW: 228.2). APS is an initiator for gel formation.
• TEMED (N, N, N', N'-tetramethylethylenediamine) (C6H16N2; mW: 116.21). Chemical polymerisation of
acrylamide gel is used for SDS-PAGE. It can be initiated by ammonium persulfate and the quaternary amine,
N,N,N',N'-tetramethylethylenediamine (TEMED). The rate of polymerisation and the properties of the resulting
gel depends on the concentration of APS and TEMED. Increasing the amount of APS and TEMED results in a
decrease in the average polymer chain length, an increase in gel turbidity and a decrease in gel elasticity.
Decreasing the amount of initiators shows the reverse effect. The lowest catalytic concentrations that will allow
polymerisation in the optimal period of time should be used. APS and TEMED are used, approximately in
equimolar concentrations in the range of 1 to 10 mM.

Chemicals for processing and visualization

The following chemicals are used for processing of the gel and the protein samples visualized in it:
• Bromophenol blue (BPB) (3',3",5',5" tetrabromophenolsulfonphthalein) (C19H10Br4O5S; mW: 669.99). BPB
is the universal marker dye. Proteins and nucleic acids are mostly colourless. When they are subjected to
electrophoresis, it is important to stop the run before they run off the gel. BPB is the most commonly employed
tracking dye, because it is viable in alkali and neutral pH, it is a small molecule, it is ionisable and it is negatively
charged above pH 4.6 and hence moves towards the anode. Being a small molecule it moves ahead of most
proteins and nucleic acids. As it reaches the anodic end of the electrophoresis medium electrophoresis is stopped.
It can bind with proteins weakly and give blue colour.
• Glycerol (C3H8O3; mW: 92.09). It is a preservative and a weighing agent. Addition of glycerol (20-30 or 50%)
is often recommended for the storage of enzymes. Glycerol maintains the protein solution at very low
temperature, without freezing. It also helps to weigh down the sample into the wells without being spread while
loading.
• Coomassie Brilliant Blue R-250 (CBB)(C45H44N3NaO7S2; mW: 825.97). CBB is the most popular protein
stain. It is an anionic dye, which binds with proteins non-specifically. The structure of CBB is predominantly
non-polar. So is usually used (0.025%) in methanolic solution (40%) and acetic acid (7%). Proteins in the gel are
fixed by acetic acid and simultaneously stained. The excess dye incorporated in the gel can be removed by
destaining with the same solution but without the dye. The proteins are detected as blue bands on a clear
background. As SDS is also anionic, it may interfere with staining process. Therefore, large volume of staining
solution is recommended, approximately ten times the volume of the gel.
• n-Butanol (C4H10O; mW: 74.12). Water saturated butanol is used as an overlay solution on the resolving gel.
• Dithiothreitol (DTT; C4H10O2S2; mW: 154.25). DTT is a reducing agent used to disrupt disulfide bonds to
ensure the protein is fully denatured before loading on the gel; ensuring the protein runs uniformly. Traditionally
the toxic and less potent 2-mercaptoethanol was used.

Reducing SDS-PAGE
Besides the addition of SDS, proteins may optionally be briefly heated to near boiling in the presence of a reducing
agent, such as dithiothreitol (DTT) or traditionally 2-mercaptoethanol (beta-mercaptoethanol/BME), which further
denatures the proteins by reducing disulfide linkages, thus overcoming some forms of tertiary protein folding, and
breaking up quaternary protein structure (oligomeric subunits). This is known as reducing SDS-PAGE, and is most
commonly used. Non-reducing SDS-PAGE (no boiling and no reducing agent) may be used when native structure is
important in further analysis (e.g. enzyme activity, shown by the use of zymograms). For example, quantitative
preparative native continuous polyacrylamide gel electrophoresis (QPNC-PAGE) is a new method for separating
native metalloproteins in complex biological matrices.
SDS-PAGE 7

Silver staining
In the 14th century the silver staining technique was developed for colouring the
surface of glass. It has been used extensively for this purpose since the 16th
century. The colour produced by the early silver stains ranged between light yellow
and an orange-red. Camillo Golgi perfected the silver staining for the study of the
nervous system. Golgi's method stains a limited number of cells at random in their
entirety.[15] The exact chemical mechanism by which this happens is still largely
unknown.[16] Silver staining was introduced by Kerenyi and Gallyas as a sensitive
procedure to detect trace amounts of proteins in gels.[17] The technique has been
extended to the study of other biological macromolecules that have been separated
in a variety of supports.[18] Classical Coomassie Brilliant Blue staining can usually
detect a 50 ng protein band, Silver staining increases the sensitivity typically 50
times. Many variables can influence the colour intensity and every protein has its
own staining characteristics; clean glassware, pure reagents and water of highest
purity are the key points to successful staining.[19]

Silver stained SDS

Polyacrylamide gels
SDS-PAGE 8

Buffer systems
Most protein separations are performed using a "discontinuous" buffer
system that significantly enhances the sharpness of the bands within
the gel. During electrophoresis in a discontinuous gel system, an ion
gradient is formed in the early stage of electrophoresis that causes all
of the proteins to focus into a single sharp band. This occurs in a region
of the gel that has larger pores so that the gel matrix does not retard the
migration during the focusing or "stacking" event. Negative ions from
the buffer in the tank then "outrun" the SDS-covered protein "stack"
and eliminate the ion gradient so that the proteins subsequently
separate by the sieving action in the lower, "resolving" region of the
gel.

Many people continue to use a tris-glycine or "Laemmli" buffering

system that stacks at a pH of 6.8 and resolves at a pH of ~8.3-9.0.
These pHs promote disulfide bond formation between cysteine
residues in the proteins, especially when they are present at high
concentrations because the pKa of cysteine ranges from 8-9 and
because reducing agent present in the loading buffer doesn't co-migrate
with the proteins. Recent advances in buffering technology alleviate Postulated migration of proteins in a Laemmli gel
this problem by resolving the proteins at a pH well below the pKa of system A: Stacking gel, B: Resolving gel, o:
sample application c: discontinuities in the buffer
cysteine (e.g., bis-tris, pH 6.5) and include reducing agents (e.g.
and electrophoretic matrix
sodium bisulfite) that move into the gel ahead of the proteins to
maintain a reducing environment. An additional benefit of using
buffers with lower pHs is that the acrylamide gel is more stable so the gels can be stored for long periods of time
before use.[20] [21]

SDS gradient gel electrophoresis of proteins

As voltage is applied, the anions (and
negatively charged sample molecules)
migrate toward the positive electrode
(anode) in the lower chamber, the leading
ion is Cl¯ ( high mobility and high
concentration); glycinate is the trailing ion
(low mobility and low concentration).
SDS-protein particles do not migrate freely
at the border between the Cl¯ of the gel
buffer and the Gly¯ of the cathode buffer.
Migration of proteins in SDS gels of varying acrylamide concentrations (%T). The Friedrich Kohlrausch found that Ohm's law
migration of nine proteins ranging from 94 kDa to 14.4 kDa is shown. Stacking also applies to dissolved electrolytes.
and unstacking occurs continuously in the gel, for every protein at a different gel
Because of the voltage drop between the Cl-
concentration. The dotted line indicates the discontinuity at the Gly¯/Cl¯ moving
boundary. Proteins between the fast leading electrolyte and the slow trailing
and Glycine-buffers, proteins are
electrolyte are not diluted by diffusion. compressed (stacked) into micrometer thin
layers. [22] The boundary moves through a
SDS-PAGE 9

pore gradient and the protein stack gradually disperses due to an frictional resistance increase of the gel matrix.
Stacking and unstacking occurs continuously in the gradient gel, for every protein at a different position. For a
complete protein unstacking the polyacrylamide-gel concentration must exceed 16% T. The two-gel system of
"Laemmli" is a simple gradient gel. The pH discontinuity of the buffers is of no significance for the separation
quality, and a "stacking-gel" with a different pH is not needed.

See also
• Capillary electrophoresis
• DNA electrophoresis
• Eastern blotting
• Electroblotting
• Electrophoresis
• Gel electrophoresis
• History of electrophoresis
• Isoelectric focusing
• Isotachophoresis
• Native Gel Electrophoresis
• Northern blotting
• Protein electrophoresis
• Southern blotting
• Two dimensional SDS-PAGE
• Western blotting
• Zymography

External links
• Demystifying SDS-PAGE Video [23]
• Demystifying SDS-PAGE [24]
• SDS-PAGE Calculator [25] for customised recipes for TRIS Urea gels.
• 2-Dimensional Protein Gelelectrophoresis [26]
• [27] Hempelmann E. SDS-Protein PAGE and Proteindetection by Silverstaining and Immunoblotting of
Plasmodium falciparum proteins. in: Moll K, Ljungström J, Perlmann H, Scherf A, Wahlgren M (eds) Methods in
Malaria Research, 5th edition, 2008, 263-266

References
[1] Shapiro AL, Viñuela E, Maizel JV Jr. (September 1967). "Molecular weight estimation of polypeptide chains by electrophoresis in
SDS-polyacrylamide gels.". Biochem Biophys Res Commun. 28 (5): 815–820. doi:10.1016/0006-291X(67)90391-9. PMID 4861258.
[2] Weber K, Osborn M (August 1969). "The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel
electrophoresis.". J Biol Chem. 244 (16): 4406–4412. PMID 5806584.
[3] Laemmli UK (August 1970). "Cleavage of structural proteins during the assembly of the head of bacteriophage T4". Nature 227 (5259):
680–685. doi:10.1038/227680a0. PMID 5432063.
[4] Caprette, David. "SDS-PAGE" (http:/ / www. ruf. rice. edu/ ~bioslabs/ studies/ sds-page/ denature. html). . Retrieved 27 Sept 2009.
[5] "What is the meaning of de -gas the acrylamide gel mix?" (http:/ / www. protocol-online. org/ biology-forums/ posts/ 17740. html). .
Retrieved 28 Sept 2009.
[6] "SDS-PAGE" (http:/ / www. science. smith. edu/ departments/ Biochem/ Biochem_353/ sdspage. html). . Retrieved 12 Sept 2009.
[7] Schägger, H; Von Jagow, G (1987). "Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the
range from 1 to 100 kDa.". Anal. Biochem. 166 (2): 368–379. doi:10.1016/0003-2697(87)90587-2. PMID 2449095.
[8] Andrews. "SDS-PAGE" (http:/ / www. dwalab. ca/ labman/ recipes/ PreparingtoRunTricineSDSGels. html). . Retrieved 27 Sept 2009.
[9] http:/ / encorbio. com/ protocols/ SDS-Calc. htm
SDS-PAGE 10

[10] Davis BJ, Ornstein L (1959). "A new high resolution electrophoresis method.". Delivered at the Society for the Study of Blood at the New
York Academy of Medicine.
[11] Raymond S, Weintraub L. (1959). "Acrylamide gel as a supporting medium for zone electrophoresis.". Science 130: 711.
doi:10.1126/science.130.3377.711. PMID 14436634.
[12] Rüchel R, Steere RL, Erbe EF (1978). "Transmission-electron microscopic observations of freeze-etched polyacrylamide gels.". J
Chromatogr. 166: 563–575. doi:10.1016/S0021-9673(00)95641-3.
[13] Ornstein L (December 1964). "DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY.". Ann N Y Acad Sci. 121: 321–349.
doi:10.1111/j.1749-6632.1964.tb14207.x. PMID 14240533.
[14] Davis BJ (December 1964). "Disc Electrophoresis. 2, Method and application to human serum proteins". Ann. New York Acad. Sci 121:
404–427. doi:10.1111/j.1749-6632.1964.tb14213.x. PMID 14240539.
[15] Grant G (Oct 2007). "How the 1906 Nobel Prize in Physiology or Medicine was shared between Golgi and Cajal". Brain Res Rev 55 (2):
490–498. doi:10.1016/j.brainresrev.2006.11.004. PMID 17306375.
[16] Golgi C (1873). "Sulla struttura della sostanza grigia del cervello.". Gazzetta Medica Italiana (Lombardia) 33: 244–246.
[17] Kerenyi L, Gallyas F (1973). "Über Probleme der quantitiven Auswertung der mit physikalischer Entwicklung versilberten
Agarelektrophoretogramme". Clin. Chim. Acta 47 (3): 425–436. doi:10.1016/0009-8981(73)90276-3. PMID 4744834.
[18] Switzer RC 3rd, Merril CR, Shifrin S (Sep 1979). "A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide
gels.". Anal Biochem. 98 (1): 231–237. doi:10.1016/0003-2697(79)90732-2. PMID 94518.
[19] Hempelmann E, Schulze M, Götze O (1984). "Free SH-groups are important for the polychromatic staining of proteins with silver nitrat".
Neuhof V (ed)Electrophoresis '84 , Verlag Chemie Weinheim 1984: 328–330.
[20] Schägger H, von Jagow G (1987). "Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the
range from 1 to 100 kDa.". Anal Biochem. 166 (2): 368–379. doi:10.1016/0003-2697(87)90587-2. PMID 2449095.
[21] Wiltfang J, Arold N, Neuhoff V (1991). "A new multiphasic buffer system for sodium dodecyl sulfate-polyacrylamide gel electrophoresis of
proteins and peptides with molecular masses 100,000-1000, and their detection with picomolar sensitivity.". Electrophoresis 12 (5): 352–366.
doi:10.1002/elps.1150120507. PMID 1718736.
[22] Kohlrausch F (1897). "Ueber Concentrations-Verschiebungen durch Electrolyse im Inneren von Lösungen und Lösungsgemischen.".
Ann.J.Phys.u.Chem. 62: 209–239. doi:10.1002/andp.18972981002.
[23] http:/ / sdspage. homestead. com/ TheVideo. html
[24] http:/ / sdspage. homestead. com/
[25] http:/ / www. omx-online. com/ calculator. html
[26] http:/ / wwwzb. zb. kfa-juelich. de/ wiki/ index. php?title=Sample_preparation_2D
[27] http:/ / www. biomalpar. org/ updatedMethods_In_Malaria_Research_5thedition. pdf
Article Sources and Contributors 11

Article Sources and Contributors

SDS-PAGE  Source: http://en.wikipedia.org/w/index.php?oldid=374655002  Contributors: Aa77zz, Aciel, Ahoerstemeier, Andrewrp, Arc de Ciel, Bender235, Benjicharlton, Bensaccount,
Biochemza, BrewBelly, Brianoflee, Bryan Derksen, CZmarlin, Chaiken, Choanoflagellate, Closedmouth, CommonsDelinker, Cst17, Damnable123, David Munch, Discospinster, Dnapurifier,
Eganio, Eykanal, Fabiform, GerryShaw, Gkrajeshrajesh, Graft, Graham87, Gustavocarra, Heathmoor, Hempelmann, Herbal Lemon, Hillarryous, Horst, I.D.10-t, J.delanoy, JOK, Jaganath,
Japanese Searobin, Jepoirrier, Jimtassano, Julianonions, Justinm704, Jwfowble, Kierano, Kkmurray, Kupirijo, Lexor, Lightmouse, Likeitsmyjob, Lord Anubis, Lordmetroid, LostLucidity, MC10,
Magnus Manske, Marshman, Mav, Mephistophelian, Michael Hardy, MichaelJanich, Nrusimhanathmisra, Orthank, PDH, Papercutbiology, Pdcook, Pharamund, Proteinwizard, Qchristensen,
R'n'B, Ravi.patil30, Rjwilmsi, Roadnottaken, Robbrad3, RogueNinja, Rrburke, Rss100001, Sakkura, Seans Potato Business, Seonaidmargaret, Sfan00 IMG, SquidDNA, Sriram sh, Stephenb,
Temporaluser, Terminator1000, Theone00, TimVickers, Tirkfl, Tregoweth, TutterMouse, UW, Wedian, Wintan29, Ww2censor, XApple, Xaosflux, Yasha, Yerpo, Zafiroblue05, 151 anonymous
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