148:. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) is a method of separating molecules based on the difference of their molecular weight. At the pH at which gel electrophoresis is carried out the SDS molecules are negatively charged and bind to proteins in a set ratio, approximately one molecule of SDS for every 2 amino acids. In this way, the detergent provides all proteins with a uniform charge-to-mass ratio. By binding to the proteins the detergent destroys their secondary, tertiary and/or quaternary structure denaturing them and turning them into negatively charged linear polypeptide chains. When subjected to an electric field in PAGE, the negatively charged polypeptide chains travel toward the anode with different mobility. Their mobility, or the distance traveled by molecules, is inversely proportional to the logarithm of their molecular weight. By comparing the relative ratio of the distance traveled by each protein to the length of the gel (Rf) one can make conclusions about the relative molecular weight of the proteins, where the length of the gel is determined by the distance traveled by a small molecule like a tracking dye.
349:
Depending on their size, each biomolecule moves differently through the gel matrix: small molecules more easily fit through the pores in the gel, while larger ones have more difficulty. The gel is run usually for a few hours, though this depends on the voltage applied across the gel; migration occurs more quickly at higher voltages, but these results are typically less accurate than at those at lower voltages. After the set amount of time, the biomolecules have migrated different distances based on their size. Smaller biomolecules travel farther down the gel, while larger ones remain closer to the point of origin. Biomolecules may therefore be separated roughly according to size, which depends mainly on molecular weight under denaturing conditions, but also depends on higher-order conformation under native conditions. The gel mobility is defined as the rate of migration traveled with a voltage gradient of 1V/cm and has units of cm/sec/V. For analytical purposes, the relative mobility of biomolecules,
433:
strong, chemically relatively inert gel, and can be prepared with a wide range of average pore sizes. The pore size of a gel and the reproducibility in gel pore size are determined by three factors, the total amount of acrylamide present (%T) (T = Total concentration of acrylamide and bisacrylamide monomer), the amount of cross-linker (%C) (C = bisacrylamide concentration), and the time of polymerization of acrylamide (cf. QPNC-PAGE). Pore size decreases with increasing %T; with cross-linking, 5%C gives the smallest pore size. Any increase or decrease in %C from 5% 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 non-homogeneous bundling of polymer strands within the gel. This gel material can also withstand high
128:. Acrylamide monomer is in a powder state before addition of water. Acrylamide is toxic to the human nervous system, therefore all safety measures must be followed when working with it. Acrylamide is soluble in water and upon addition of free-radical initiators it polymerizes resulting in formation of polyacrylamide. It is useful to make polyacrylamide gel via acrylamide hydration because pore size can be regulated. Increased concentrations of acrylamide result in decreased pore size after polymerization. Polyacrylamide gel with small pores helps to examine smaller molecules better since the small molecules can enter the pores and travel through the gel while large molecules get trapped at the pore openings.
292:, which can form cross-links between two acrylamide molecules. The ratio of bisacrylamide to acrylamide can be varied for special purposes, but is generally about 1 part in 35. 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 molecules, while much higher percentages of acrylamide are needed to resolve smaller proteins. The average pore diameter of polyacrylamide gels is determined by the total concentration of acrylamides (% T with T = Total concentration of acrylamide and bisacrylamide) and the concentration of the
211:
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725:; mW: 116.21) stabilizes free radicals and improves polymerization. The rate of polymerisation and the properties of the resulting gel depend on the concentrations of free radicals. Increasing the amount of free radicals results in a decrease in the average polymer chain length, an increase in gel turbidity and a decrease in gel elasticity. Decreasing the amount shows the reverse effect. The lowest
376:
280:, the optional denaturant (SDS or urea), and a buffer with an adjusted pH. The solution may be degassed under a vacuum to prevent the formation of air bubbles during polymerization. Alternatively, butanol may be added to the resolving gel (for proteins) after it is poured, as butanol removes bubbles and makes the surface smooth. A source of free radicals and a stabilizer, such as
841:
The proteins are fixed to the gel with a dilute methanol solution, then incubated with an acidic silver nitrate solution. Silver ions are reduced to their metallic form by formaldehyde at alkaline pH. An acidic solution, such as acetic acid stops development. Silver staining was introduced by
Kerenyi and Gallyas as a sensitive procedure to detect trace amounts of proteins in
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169:
the oligomeric form intact and will show a band on the gel that is representative of the level of activity. SDS-PAGE will denature and separate the oligomeric form into its monomers, showing bands that are representative of their molecular weights. These bands can be used to identify and assess the purity of the protein.
597:. This denaturation, which is referred to as reconstructive denaturation, is not accomplished by the total linearization of the protein, but instead, through a conformational change to a combination of random coil and α helix secondary structures. When a protein mixture is heated to 100 °C in presence of SDS, the
450:
faster protein mobility. Separating gels have a pH of 8.8, where the anionic glycine slows down the mobility of proteins. Separating gels allow for the separation of proteins and have a relatively lower porosity. Here, the proteins are separated based on size (in SDS-PAGE) and size/ charge (Native PAGE).
410:
For proteins, SDS-PAGE is usually the first choice as an assay of purity due to its reliability and ease. The presence of SDS and the denaturing step make proteins separate, approximately based on size, but aberrant migration of some proteins may occur. Different proteins may also stain differently,
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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. Silver staining was developed in the 14th century for colouring the surface of glass. It has been used extensively for this purpose
182:
Samples may be any material containing proteins or nucleic acids. These may be biologically derived, for example from prokaryotic or eukaryotic cells, tissues, viruses, environmental samples, or purified proteins. In the case of solid tissues or cells, these are often first broken down mechanically
163:
may also be used to disrupt the disulfide bonds found between the protein complexes, which helps further denature the protein. In most proteins, the binding of SDS to the polypeptide chains impart an even distribution of charge per unit mass, thereby resulting in a fractionation by approximate size
840:
Silver staining is used when more sensitive method for detection is needed, as classical
Coomassie Brilliant Blue staining can usually detect a 50 ng protein band, Silver staining increases the sensitivity typically 10-100 fold more. This is based on the chemistry of photographic development.
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in their native environment – are intrinsically harder to treat accurately using this method, due to the greater variability in the ratio of bound SDS. Procedurally, using both Native and SDS-PAGE together can be used to purify and to separate the various subunits of the protein. Native-PAGE keeps
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solution acidified with acetic acid. Proteins in the gel are fixed by acetic acid and simultaneously stained. The excess dye incorporated into the gel can be removed by destaining with the same solution without the dye. The proteins are detected as blue bands on a clear background. As SDS is also
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Polyacrylamide gels are composed of a stacking gel and separating gel. Stacking gels have a higher porosity relative to the separating gel, and allow for proteins to migrate in a concentrated area. Additionally, stacking gels usually have a pH of 6.8, since the neutral glycine molecules allow for
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and thereby the resolution of the gel. The buffer should also be unreactive and not modify or react with most proteins. Different buffers may be used as cathode and anode buffers, respectively, depending on the application. Multiple pH values may be used within a single gel, for example in DISC
432:
had been known as a potential embedding medium for sectioning tissues as early as 1964, and two independent groups employed PAG in electrophoresis in 1959. It possesses several electrophoretically desirable features that make it a versatile medium. It is a synthetic, thermo-stable, transparent,
601:
wraps around the polypeptide backbone. It binds to polypeptides in a constant weight ratio of 1.4 g SDS/g of polypeptide. In this process, the intrinsic charges of polypeptides become negligible when compared to the negative charges contributed by SDS. Thus polypeptides after treatment become
571:; mW: 154.17) is the most frequently used cross linking agent for polyacrylamide gels. Chemically it can be thought of as two acrylamide molecules coupled head to head at their non-reactive ends. Bisacrylamide can crosslink two polyacrylamide chains to one another, thereby resulting in a gel.
480:
during electrophoresis. Highly charged and mobile ions are often avoided in SDS-PAGE cathode buffers, but may be included in the gel itself, where it migrates ahead of the protein. In applications such as DISC SDS-PAGE the pH values within the gel may vary to change the average charge of the
348:
An electric field is applied across the gel, causing the negatively charged proteins or nucleic acids to migrate across the gel away from the negative electrode (which is the cathode being that this is an electrolytic rather than galvanic cell) and towards the positive electrode (the anode).
752:
Tracking dye; as proteins and nucleic acids are mostly colorless, their progress through the gel during electrophoresis cannot be easily followed. Anionic dyes of a known electrophoretic mobility are therefore usually included in the PAGE sample buffer. A very common tracking dye is
837:. Because of this fact, many researchers opt to use stains such as SYBR Green and SYBR Safe which are safer alternatives to EtBr. EtBr is used by simply adding it to the gel mixture. Once the gel has run, the gel may be viewed through the use of a photo-documentation system.
143:
Alternatively, a chemical denaturant may be added to remove this structure and turn the molecule into an unstructured molecule whose mobility depends only on its length (because the protein-SDS complexes all have a similar mass-to-charge ratio). This procedure is called
367:, however, behave anomalously on SDS gels. Additionally, the analysis of larger proteins ranging from 250,000 to 600,000 Da is also reported to be problematic due to the fact that such polypeptides move improperly in the normally used gel systems.
2177:
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,
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bisacrylamide (%C with C = bisacrylamide concentration). The pore size is reduced reciprocally to the %T. Concerning %C, a concentration of 5% produces the smallest pores, since the influence of bisacrylamide on the pore size has a
253:, 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.
256:
A tracking dye may be added to the solution. This typically has a higher electrophoretic mobility than the analytes to allow the experimenter to track the progress of the solution through the gel during the electrophoretic run.
44:
315:
Gels are usually polymerized between two glass plates in a gel caster, with a comb inserted at the top to create the sample wells. After the gel is polymerized the comb can be removed and the gel is ready for electrophoresis.
489:. 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
829:(EtBr) is a popular nucleic acid stain. EtBr allows one to easily visualize DNA or RNA on a gel as EtBr fluoresces an orange color under UV light. Ethidium bromide binds nucleic acid chains through the process of
1820:
Singer VL, Lawlor TE, Yue S (1999). "Comparison of SYBR Green I nucleic acid gel stain mutagenicity and ethidium bromide mutagenicity in the
Salmonella/mammalian microsome reverse mutation assay (Ames test)".
356:, the ratio of the distance the molecule traveled on the gel to the total travel distance of a tracking dye is plotted versus the molecular weight of the molecule (or sometimes the log of MW, or rather the M
776:
Loading aids; most PAGE systems are loaded from the top into wells within the gel. To ensure that the sample sinks to the bottom of the gel, sample buffer is supplemented with additives that increase the
526:. 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 linking various chains together. Acrylamide is
98:
gel electrophoresis is a powerful tool used to analyze RNA samples. When polyacrylamide gel is denatured after electrophoresis, it provides information on the sample composition of the RNA species.
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membrane. It is then possible to apply immunochemical techniques to visualise the transferred proteins, as well as accurately identify relative increases or decreases of the protein of interest.
729:
concentrations that allow polymerisation in a reasonable period of time should be used. APS and TEMED are typically used at approximately equimolar concentrations in the range of 1 to 10 mM.
360:, molecular radius). Such typically linear plots represent the standard markers or calibration curves that are widely used for the quantitative estimation of a variety of biomolecular sizes.
159:(SDS) is an anionic detergent applied to protein samples to coat proteins in order to impart two negative charges (from every SDS molecule) to every two amino acids of the denatured protein.
818:; mW: 825.97) is the most popular protein stain. It is an anionic dye, which non-specifically binds to proteins. The structure of CBB is predominantly non-polar, and it is usually used in
238:
secondary and non–disulfide–linked tertiary structures, and additionally applies a negative charge to each protein in proportion to its mass. Urea breaks the hydrogen bonds between the
602:
rod-like structures possessing a uniform charge density, that is same net negative charge per unit weight. The electrophoretic mobilities of these proteins is a linear function of the
331:
Various buffer systems are used in PAGE depending on the nature of the sample and the experimental objective. The buffers used at the anode and cathode may be the same or different.
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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
457:
stabilizes the pH value to the desired value within the gel itself and in the electrophoresis buffer. The choice of buffer also affects the electrophoretic mobility of the buffer
31:
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1239:
869:
Autoradiography, also used for protein band detection post gel electrophoresis, uses radioactive isotopes to label proteins, which are then detected by using X-ray film.
2021:
Song D, Ma S, Khor SP (2002). "Gel electrophoresis-autoradiographic image analysis of radiolabeled protein drug concentration in serum for pharmacokinetic studies".
1679:
Duchesne LG, Lam JS, MacDonald LA, et al. (1988). "Effect of pH and acrylamide concentration on the separation of lipopolysaccharides in polyacrylamide gels".
1183:
757:(BPB, 3',3",5',5" tetrabromophenolsulfonphthalein). This dye is coloured at alkali and neutral pH and is a small negatively charged molecule that moves towards the
1479:
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".
655:. Macromolecular structure is dependent on the net effect of these forces, therefore it follows that an increase in chaotropic solutes denatures macromolecules,
765:
end of the electrophoresis medium electrophoresis is stopped. It can weakly bind to some proteins and impart a blue colour. Other common tracking dyes are
1546:
Quandt N, Stindl A, Keller U (1993). "Sodium
Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis for Mr Estimations of High-Molecular-Weight Polypeptides".
2364:
1961:
Hempelmann E, Schulze M, Götze O (1984). "Free SH-groups are important for the polychromatic staining of proteins with silver nitrat". In Neuhof V (ed.).
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anionic, it may interfere with staining process. Therefore, large volume of staining solution is recommended, at least ten times the volume of the gel.
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of the sample. These additives should be non-ionic and non-reactive towards proteins to avoid interfering with electrophoresis. Common additives are
618:. 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.
2605:
2451:
1516:
2170:
1890:
Kerenyi L, Gallyas F (1973). "Ăśber
Probleme der quantitiven Auswertung der mit physikalischer Entwicklung versilberten Agarelektrophoretogramme".
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which interferes with quantification by staining. PAGE may also be used as a preparative technique for the purification of proteins. For example,
309:
342:
320:
2446:
1237:
Shapiro AL, Viñuela E, Maizel JV Jr (1967). "Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels".
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is a process by which proteins separated in the acrylamide gel are electrophoretically transferred to a stable, manipulable membrane such as a
164:
during electrophoresis. Proteins that have a greater hydrophobic content – for instance, many membrane proteins, and those that interact with
2743:
1866:
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1100:
1008:
991:
Petrov A, Tsa A, Puglisi JD (2013). "Chapter
Sixteen – Analysis of RNA by Analytical Polyacrylamide Gel Electrophoresis". In Lorsch J (ed.).
195:
or by using cycling of high pressure, and a combination of biochemical and mechanical techniques – including various types of filtration and
242:
of the nucleic acid, causing the constituent strands to separate. Heating the samples to at least 60 °C further promotes denaturation.
2636:
2565:
2120:
1925:
Switzer RC 3rd, Merril CR, Shifrin S (1979). "A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels".
680:; mW: 228.2) is a source of free radicals and is often used as an initiator for gel formation. An alternative source of free radicals is
335:
2631:
2610:
1279:
261:
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gradients, is amenable to various staining and destaining procedures, and can be digested to extract separated fractions or dried for
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of acrylamide takes place, joining molecules together by head on tail fashion to form long single-chain polymers. The presence of a
534:, and a reproductive toxin. It is also essential to store acrylamide in a cool dark and dry place to reduce autopolymerisation and
2600:
2301:
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593:; mW: 288.38) (only used in denaturing protein gels) is a strong detergent agent used to denature native proteins to individual
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2590:
2530:
2262:
1716:
2545:
2139:
1650:
RĂĽchel R, Steere RL, Erbe EF (1978). "Transmission-electron microscopic observations of freeze-etched polyacrylamide gels".
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RĂĽchel R, Steere RL, Erbe EF (1978). "Transmission-electron microscopic observations of freeze-etched polyacrylamide gels".
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In addition to SDS, proteins may optionally be briefly heated to near boiling in the presence of a reducing agent, such as
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830:
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since the 16th century. The colour produced by the early silver stains ranged between light yellow and an orange-red.
235:
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The following chemicals and procedures are used for processing of the gel and the protein samples visualized in it.
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While
Ethidium bromide is a popular stain it is important to exercise caution when using EtBr as it is a known
792:
399:). After staining, different species biomolecules appear as distinct bands within the gel. It is common to run
384:
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of known molecular weight in a separate lane in the gel to calibrate the gel and determine the approximate
2387:
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1978:
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Laemmli UK (1970). "Cleavage of structural proteins during the assembly of the head of bacteriophage T4".
1275:"The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis"
574:
392:
227:
156:
1976:
Grant G (2007). "How the 1906 Nobel Prize in
Physiology or Medicine was shared between Golgi and Cajal".
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are added to initiate polymerization. The polymerization reaction creates a gel because of the added
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94:. Electrophoretic mobility is a function of the length, conformation, and charge of the molecule.
2253:
2003:
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Raymond S, Weintraub L (1959). "Acrylamide gel as a supporting medium for zone electrophoresis".
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The sample to analyze is optionally mixed with a chemical denaturant if so desired, usually
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2058:"Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp"
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Tareke E, Rydberg P, Eriksson S, et al. (2000). "Acrylamide: a cooking carcinogen?".
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519:-generating system greatly accelerates polymerization. This kind of reaction is known as
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that have been separated in a variety of supports. Many variables can influence the
761:. Being a highly mobile molecule it moves ahead of most proteins. As it reaches the
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Following electrophoresis, the gel may be stained (for proteins, most commonly with
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Delivered at the
Society for the Study of Blood at the New York Academy of Medicine
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of unknown biomolecules by comparing the distance traveled relative to the marker.
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395:), allowing visualization of the separated proteins, or processed further (e.g.
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1179:"Detergent binding explains anomalous SDS-PAGE migration of membrane proteins"
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of the system by interfering with intramolecular interactions mediated by non-
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Handbook of biological dyes and stains: synthesis and industrial applications
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Davis BJ, Ornstein L (1959). "A new high resolution electrophoresis method".
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Picture of an SDS-PAGE. The molecular markers (ladder) are in the left lane
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counterions during the run to improve resolution. Popular counterions are
139:, preserving the molecules' higher-order structure. This method is called
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Fundamental laboratory approaches for biochemistry and biotechnology
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LoPachin R (2004). "The changing view of acrylamide neurotoxicity".
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Fundamental Laboratory Approaches for Biochemistry and Biotechnology
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in the pH range. The minimum pH of this range is approximately 8.0.
43:
30:"PAGE" redirects here. For the Obama Administration initiative, see
845:. The technique has been extended to the study of other biological
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balance the intrinsic charge of the buffer ion and also affect the
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1153:. New Delhi: I.K. International Publishing House. p. 137.
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stains a limited number of cells at random in their entirety.
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511:; mW: 71.08) when dissolved in water, slow, spontaneous auto
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333:
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for proteins or urea for nucleic acids. SDS is an anionic
199:– may be used to separate different cell compartments and
1095:(2nd ed.). Hoboken, NJ: John Wiley & Sons, Inc.
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prior to electrophoresis. Synthetic biomolecules such as
1399:"What is the meaning of de -gas the acrylamide gel mix?"
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Rath A, Glibowicka M, Nadeau VG, et al. (2009).
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Journal of Pharmacological and Toxicological Methods
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is the most commonly used denaturant. For proteins,
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Presidential Ambassadors for Global Entrepreneurship
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1128:. New York: W.H. Freeman and Company. p. 553.
995:. Vol. 530. Academic Press. pp. 301–313.
858:perfected the silver staining for the study of the
1035:The Editors of Encyclopaedia Britannica (2017).
462:electrophoresis. Common buffers in PAGE include
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387:R-250 or autoradiography; for nucleic acids,
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251:2-mercaptoethanol (beta-mercaptoethanol/BME)
1965:. Weinheim: Verlag Chemie. pp. 328–30.
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2167:for customised recipes for TRIS Urea gels.
733:Chemicals for processing and visualization
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2606:Temperature gradient gel electrophoresis
2171:2-Dimensional Protein Gelelectrophoresis
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610:and molecular weight particular to its
379:Two SDS-PAGE-gels after a completed run
2447:Photoactivated localization microscopy
2365:Protein–protein interaction prediction
1124:Kindt T, Goldsby R, Osborne B (2007).
1091:Ninfa AJ, Ballou DP, Benore M (2010).
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684:, which generated free radicals in a
187:(for larger sample volumes), using a
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2637:Gel electrophoresis of nucleic acids
2566:Electrophoretic mobility shift assay
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423:Chemical ingredients and their roles
2632:DNA separation by silica adsorption
2611:Two-dimensional gel electrophoresis
2322:Freeze-fracture electron microscopy
2596:Polyacrylamide gel electrophoresis
2126:Polyacrylamide gel electrophoresis
1041:Britannica Online Academic Edition
1001:10.1016/B978-0-12-420037-1.00016-6
922:Fast parallel proteolysis (FASTpp)
415:is a method for separating native
52:Polyacrylamide gel electrophoresis
25:
1992:10.1016/j.brainresrev.2006.11.004
1861:. Hoboken, NJ: Wiley & Sons.
2708:
2697:
2696:
2601:Pulsed-field gel electrophoresis
2302:Isothermal titration calorimetry
2282:Dual-polarization interferometry
1791:. Hoboken, NJ: Wiley-Blackwell.
769:, which has lower mobility, and
419:in complex biological matrices.
135:, molecules may be run in their
58:) is a technique widely used in
2642:Gel electrophoresis of proteins
2591:Moving-boundary electrophoresis
2531:Capillary electrochromatography
773:, which has a higher mobility.
710:′-tetramethylethylenediamine) (
2546:Difference gel electrophoresis
1240:Biochem. Biophys. Res. Commun.
272:The gels typically consist of
207:may also be used as analytes.
1:
2647:Serum protein electrophoresis
2551:Discontinuous electrophoresis
2292:Chromatin immunoprecipitation
2035:10.1016/s1056-8719(02)00203-4
1836:10.1016/s1383-5718(98)00172-7
1666:10.1016/S0021-9673(00)95641-3
1466:10.1016/S0021-9673(00)95641-3
1294:10.1016/S0021-9258(18)94333-4
1184:Proc. Natl. Acad. Sci. U.S.A.
401:molecular weight size markers
2744:Molecular biology techniques
2355:Protein structural alignment
2340:Protein structure prediction
2140:Resources in other libraries
2085:10.1371/journal.pone.0046147
1940:10.1016/0003-2697(79)90732-2
1904:10.1016/0009-8981(73)90276-3
1857:Ninfa AJ, Ballou DP (2004).
1621:10.1126/science.130.3377.711
1494:10.1016/0003-2697(87)90587-2
1252:10.1016/0006-291X(67)90391-9
2526:Agarose gel electrophoresis
2439:Super-resolution microscopy
2345:Protein function prediction
2273:Peptide mass fingerprinting
2268:Protein immunoprecipitation
2155:Demystifying SDS-PAGE Video
1766:10.1016/j.neuro.2004.01.004
1149:Kumar A, Awasthi A (2009).
897:Agarose gel electrophoresis
2765:
2505:History of electrophoresis
1273:Weber K, Osborn M (1969).
942:Native gel electrophoresis
927:History of electrophoresis
218:by DTT via two sequential
29:
2692:
2684:Electrophoresis (journal)
2536:Capillary electrophoresis
2500:
2297:Surface plasmon resonance
2287:Microscale thermophoresis
2277:Protein mass spectrometry
2239:Green fluorescent protein
2135:Resources in your library
1151:Bioseparation Engineering
902:Capillary electrophoresis
441:and permanent recording.
268:Preparing acrylamide gels
2521:Affinity electrophoresis
2317:Cryo-electron microscopy
1378:Experimental Biosciences
967:Two dimensional SDS-PAGE
793:Coomassie brilliant blue
550:′-Methylenebisacrylamide
429:Polyacrylamide gel (PAG)
385:Coomassie brilliant blue
220:thiol-disulfide exchange
108:results in formation of
92:electrophoretic mobility
2350:Protein–protein docking
2263:Protein electrophoresis
1205:10.1073/pnas.0813167106
1045:Encyclopedia Britannica
952:Protein electrophoresis
524:addition polymerisation
478:electric field strength
413:preparative native PAGE
214:Reduction of a typical
78:to separate biological
2249:Protein immunostaining
2150:SDS-PAGE: How it Works
1561:10.1006/abio.1993.1527
746:
575:Sodium dodecyl sulfate
380:
345:
338:
323:
312:
264:
223:
191:(smaller volumes), by
157:sodium dodecyl sulfate
48:
34:. For other uses, see
2576:Immunoelectrophoresis
2561:Electrochromatography
2307:X-ray crystallography
2160:Demystifying SDS-PAGE
993:Methods in Enzymology
740:
378:
344:
337:
322:
311:
263:
213:
131:As with all forms of
90:, according to their
46:
2722:Analytical Chemistry
2668:Isoelectric focusing
2234:Protein purification
1681:Current Microbiology
932:Isoelectric focusing
653:van der Waals forces
27:Analytical technique
2663:Electrical mobility
2571:Gel electrophoresis
2259:Gel electrophoresis
2165:SDS-PAGE Calculator
2076:2012PLoSO...746147M
1963:Electrophoresis '84
1717:Chem. Res. Toxicol.
1613:1959Sci...130..711R
1431:on 20 February 2014
1335:1970Natur.227..680L
1196:2009PNAS..106.1760R
907:DNA electrophoresis
659:Ammonium persulfate
639:that increases the
614:. This is known as
282:ammonium persulfate
151:For nucleic acids,
133:gel electrophoresis
2402:Display techniques
2254:Protein sequencing
1787:Sabnis RW (2010).
1693:10.1007/BF01568528
1515:Ancrews D (2007).
1063:has generic name (
747:
635:; mW: 60.06) is a
381:
371:Further processing
346:
339:
324:
313:
265:
224:
178:Sample preparation
64:forensic chemistry
49:
18:Polyacrylamide gel
2731:
2730:
2541:Dielectrophoresis
2460:
2459:
2409:Bacterial display
2121:Library resources
2056:Minde DP (2012).
1868:978-1-891786-00-6
1798:978-0-470-40753-0
1729:10.1021/tx9901938
1135:978-1-4292-0211-4
1102:978-0-470-08766-4
1010:978-0-12-420037-1
962:Southern blotting
947:Northern blotting
612:primary structure
608:isoelectric point
391:; or for either,
161:2-Mercaptoethanol
126:nitrile hydratase
72:molecular biology
16:(Redirected from
2756:
2712:
2711:
2700:
2699:
2586:Isotachophoresis
2487:
2480:
2473:
2464:
2424:Ribosome display
2360:Protein ontology
2206:
2199:
2192:
2183:
2108:
2107:
2097:
2087:
2053:
2047:
2046:
2018:
2012:
2011:
1973:
1967:
1966:
1958:
1952:
1951:
1922:
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1892:Clin. Chim. Acta
1887:
1881:
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1676:
1670:
1669:
1653:J. Chromatogr. A
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1640:
1594:
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1537:
1536:
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1523:. Archived from
1512:
1506:
1505:
1476:
1470:
1469:
1453:J. Chromatogr. A
1447:
1441:
1440:
1438:
1436:
1427:. Archived from
1421:
1415:
1414:
1412:
1410:
1395:
1389:
1388:
1386:
1384:
1369:
1363:
1362:
1343:10.1038/227680a0
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1069:
1068:
1062:
1058:
1056:
1048:
1037:"Polyacrylamide"
1032:
1023:
1022:
988:
937:Isotachophoresis
912:Eastern blotting
873:Western blotting
827:Ethidium bromide
817:
755:Bromophenol blue
724:
679:
637:chaotropic agent
634:
592:
570:
510:
389:ethidium bromide
205:oligonucleotides
123:
21:
2764:
2763:
2759:
2758:
2757:
2755:
2754:
2753:
2749:Electrophoresis
2734:
2733:
2732:
2727:
2688:
2672:
2651:
2615:
2556:Electroblotting
2509:
2496:
2494:Electrophoresis
2491:
2461:
2456:
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2397:
2393:Secretion assay
2369:
2326:
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2020:
2019:
2015:
1975:
1974:
1970:
1960:
1959:
1955:
1924:
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1889:
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1884:
1869:
1856:
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1851:
1819:
1818:
1814:
1799:
1786:
1785:
1781:
1753:Neurotoxicology
1749:
1748:
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1713:
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1708:
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1673:
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1449:
1448:
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1422:
1418:
1408:
1406:
1403:Protocol Online
1397:
1396:
1392:
1382:
1380:
1371:
1370:
1366:
1329:(5259): 680–5.
1318:
1317:
1310:
1287:(16): 4406–12.
1272:
1271:
1267:
1236:
1235:
1231:
1176:
1175:
1168:
1161:
1148:
1147:
1143:
1136:
1126:Kuby Immunology
1123:
1122:
1118:
1103:
1090:
1089:
1072:
1059:
1049:
1034:
1033:
1026:
1011:
990:
989:
985:
980:
917:Electroblotting
893:
816:
812:
808:
804:
800:
796:
735:
723:
719:
715:
711:
678:
674:
670:
666:
662:
647:forces such as
633:
629:
625:
590:
586:
582:
578:
569:
565:
561:
557:
553:
541:Bisacrylamide (
508:
504:
500:
491:negative charge
466:, Bis-Tris, or
447:
439:autoradiography
425:
417:metalloproteins
373:
359:
354:
329:
327:Electrophoresis
270:
180:
175:
121:
117:
113:
39:
28:
23:
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15:
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5:
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2336:
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2332:Bioinformatics
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2116:
2115:External links
2113:
2110:
2109:
2070:(10): e46147.
2048:
2013:
1968:
1953:
1928:Anal. Biochem.
1917:
1898:(3): 425–436.
1882:
1867:
1849:
1812:
1797:
1779:
1742:
1706:
1671:
1642:
1589:
1574:
1555:(2): 490–494.
1549:Anal. Biochem.
1538:
1527:on 2 July 2017
1507:
1488:(2): 368–379.
1482:Anal. Biochem.
1471:
1460:(2): 563–575.
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919:
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904:
899:
892:
889:
877:nitrocellulose
864:Golgi's method
860:nervous system
847:macromolecules
831:Intercalation.
734:
731:
649:hydrogen bonds
513:polymerization
446:
443:
424:
421:
405:molecular mass
372:
369:
357:
352:
328:
325:
301:-shape with a
269:
266:
247:dithiothreitol
216:disulfide bond
197:centrifugation
179:
176:
174:
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96:Polyacrylamide
80:macromolecules
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2630:
2628:
2627:DNA laddering
2625:
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2618:
2612:
2609:
2607:
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2602:
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2581:Iontophoresis
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2445:
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2430:
2429:Yeast display
2427:
2425:
2422:
2420:
2419:Phage display
2417:
2415:
2412:
2410:
2407:
2406:
2404:
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2394:
2391:
2389:
2388:Protein assay
2386:
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2376:
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2255:
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2250:
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2245:
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2240:
2237:
2235:
2232:
2231:
2229:
2227:
2223:
2218:
2214:
2207:
2202:
2200:
2195:
2193:
2188:
2187:
2184:
2176:
2174:
2172:
2169:
2166:
2163:
2161:
2158:
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2148:
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2127:
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2105:
2101:
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2091:
2086:
2081:
2077:
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2069:
2065:
2064:
2059:
2052:
2049:
2044:
2040:
2036:
2032:
2028:
2024:
2017:
2014:
2009:
2005:
2001:
1997:
1993:
1989:
1985:
1981:
1980:
1979:Brain Res Rev
1972:
1969:
1964:
1957:
1954:
1949:
1945:
1941:
1937:
1933:
1930:
1929:
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1918:
1913:
1909:
1905:
1901:
1897:
1893:
1886:
1883:
1878:
1874:
1870:
1864:
1860:
1853:
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1845:
1841:
1837:
1833:
1829:
1826:
1825:
1816:
1813:
1808:
1804:
1800:
1794:
1790:
1783:
1780:
1775:
1771:
1767:
1763:
1760:(4): 617–30.
1759:
1755:
1754:
1746:
1743:
1738:
1734:
1730:
1726:
1723:(6): 517–22.
1722:
1719:
1718:
1710:
1707:
1702:
1698:
1694:
1690:
1686:
1682:
1675:
1672:
1667:
1663:
1660:(2): 563–75.
1659:
1655:
1654:
1646:
1643:
1638:
1634:
1630:
1626:
1622:
1618:
1614:
1610:
1607:(3377): 711.
1606:
1602:
1601:
1593:
1590:
1585:
1578:
1575:
1570:
1566:
1562:
1558:
1554:
1551:
1550:
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1526:
1522:
1518:
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1443:
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1426:
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1379:
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1372:Caprette DR.
1368:
1365:
1360:
1356:
1352:
1348:
1344:
1340:
1336:
1332:
1328:
1324:
1323:
1315:
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1295:
1290:
1286:
1282:
1281:
1276:
1269:
1266:
1261:
1257:
1253:
1249:
1246:(5): 815–20.
1245:
1242:
1241:
1233:
1230:
1225:
1221:
1216:
1211:
1206:
1201:
1197:
1193:
1190:(6): 1760–5.
1189:
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1167:
1162:
1160:9789380026084
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1038:
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1002:
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905:
903:
900:
898:
895:
894:
890:
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886:
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878:
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870:
867:
865:
861:
857:
856:Camillo Golgi
852:
848:
844:
838:
836:
832:
828:
824:
821:
794:
790:
788:
784:
780:
774:
772:
768:
767:xylene cyanol
764:
760:
756:
750:
744:
739:
732:
730:
728:
709:
705:
701:
697:
693:
689:
687:
686:photochemical
683:
660:
656:
654:
650:
646:
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638:
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422:
420:
418:
414:
408:
406:
402:
398:
394:
390:
386:
377:
370:
368:
366:
365:glycoproteins
361:
355:
343:
336:
332:
326:
321:
317:
310:
306:
304:
300:
295:
291:
290:bisacrylamide
287:
283:
279:
278:bisacrylamide
275:
267:
262:
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252:
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243:
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172:
170:
167:
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154:
149:
147:
142:
138:
134:
129:
127:
111:
107:
106:acrylonitrile
103:
99:
97:
93:
89:
88:nucleic acids
85:
81:
77:
76:biotechnology
73:
69:
65:
61:
57:
53:
45:
41:
37:
33:
19:
2720:
2713:
2701:
2620:Applications
2595:
2414:mRNA display
2383:Enzyme assay
2244:Western blot
2226:Experimental
2125:
2067:
2061:
2051:
2029:(1): 59–66.
2026:
2022:
2016:
1986:(2): 490–8.
1983:
1977:
1971:
1962:
1956:
1934:(1): 231–7.
1931:
1926:
1920:
1895:
1891:
1885:
1858:
1852:
1830:(1): 37–47.
1827:
1822:
1815:
1788:
1782:
1757:
1751:
1745:
1720:
1715:
1709:
1687:(4): 191–4.
1684:
1680:
1674:
1657:
1651:
1645:
1604:
1598:
1592:
1583:
1577:
1552:
1547:
1541:
1531:27 September
1529:. Retrieved
1525:the original
1520:
1510:
1485:
1480:
1474:
1457:
1451:
1445:
1435:12 September
1433:. Retrieved
1429:the original
1419:
1409:28 September
1407:. Retrieved
1402:
1393:
1383:27 September
1381:. Retrieved
1377:
1367:
1326:
1320:
1284:
1278:
1268:
1243:
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1187:
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1150:
1144:
1125:
1119:
1092:
1040:
992:
986:
871:
868:
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825:
795:R-250 (CBB)(
791:
775:
751:
748:
707:
703:
699:
695:
690:
657:
620:
595:polypeptides
573:
547:
543:
540:
528:carcinogenic
517:free radical
495:
472:
452:
448:
428:
427:
426:
409:
397:Western blot
393:silver stain
382:
362:
350:
347:
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314:
294:cross-linker
271:
255:
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181:
150:
141:native-PAGE.
140:
137:native state
130:
100:
60:biochemistry
55:
51:
50:
40:
2452:Vertico SMI
2312:Protein NMR
1824:Mutat. Res.
1521:Andrews Lab
1280:J Biol Chem
1061:|last=
616:native PAGE
459:counterions
189:homogenizer
166:surfactants
112:molecules (
2738:Categories
2514:Techniques
1517:"SDS-PAGE"
1425:"SDS-PAGE"
1374:"SDS-PAGE"
978:References
972:Zymography
835:carcinogen
820:methanolic
688:reaction.
682:riboflavin
604:logarithms
536:hydrolysis
532:neurotoxin
497:Acrylamide
474:Counterion
445:Components
274:acrylamide
240:base pairs
222:reactions.
201:organelles
110:acrylamide
82:, usually
1877:633862582
1807:647922579
1111:420027217
1053:cite book
957:QPNC-PAGE
743:rotavirus
727:catalytic
599:detergent
468:imidazole
453:Chemical
249:(DTT) or
236:denatures
232:detergent
193:sonicator
173:Procedure
102:Hydration
2703:Category
2677:Journals
2219:of study
2213:Proteins
2104:23056252
2063:PLOS One
2043:12387940
2008:24331507
2000:17306375
1844:10029672
1774:15183015
1737:10858325
1629:14436634
1224:19181854
1019:24034328
891:See also
783:glycerol
771:Orange G
741:PAGE of
645:covalent
363:Certain
299:parabola
183:using a
146:SDS-PAGE
84:proteins
68:genetics
2715:Commons
2217:methods
2178:263-266
2095:3463568
2072:Bibcode
1912:4744834
1637:7242716
1609:Bibcode
1600:Science
1569:8109738
1502:2449095
1359:3105149
1351:5432063
1331:Bibcode
1303:5806584
1260:4861258
1215:2644111
1192:Bibcode
787:sucrose
779:density
661:(APS) (
641:entropy
577:(SDS) (
487:tricine
483:glycine
435:voltage
305:at 5%.
185:blender
2656:Theory
2215:: key
2123:about
2102:
2092:
2041:
2006:
1998:
1946:
1910:
1875:
1865:
1842:
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1795:
1772:
1735:
1701:932635
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1500:
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1357:
1349:
1322:Nature
1301:
1258:
1222:
1212:
1157:
1132:
1109:
1099:
1047:, Inc.
1017:
1007:
851:colour
763:anodic
455:buffer
303:vertex
2375:Assay
2004:S2CID
1948:94518
1697:S2CID
1633:S2CID
1355:S2CID
883:, or
881:nylon
759:anode
692:TEMED
626:CO(NH
521:vinyl
286:TEMED
234:that
124:) by
2100:PMID
2039:PMID
1996:PMID
1944:PMID
1908:PMID
1873:OCLC
1863:ISBN
1840:PMID
1803:OCLC
1793:ISBN
1770:PMID
1733:PMID
1625:PMID
1565:PMID
1533:2009
1498:PMID
1437:2009
1411:2009
1385:2009
1347:PMID
1299:PMID
1256:PMID
1220:PMID
1155:ISBN
1130:ISBN
1107:OCLC
1097:ISBN
1065:help
1015:PMID
1005:ISBN
885:PVDF
843:gels
785:and
651:and
622:Urea
530:, a
485:and
464:Tris
284:and
153:urea
74:and
56:PAGE
36:Page
2090:PMC
2080:doi
2031:doi
1988:doi
1936:doi
1900:doi
1832:doi
1828:439
1762:doi
1725:doi
1689:doi
1662:doi
1658:166
1617:doi
1605:130
1557:doi
1553:214
1490:doi
1486:166
1462:doi
1458:166
1339:doi
1327:227
1289:doi
1285:244
1248:doi
1210:PMC
1200:doi
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997:doi
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587:NaO
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