633:
4-chloro-2-2methylbenzenediazonium salt with 3-phospho-2-naphthoic acid-2'-4'-dimethyl aniline in Tris buffer. This stain is commercially sold as a kit for staining gels. If the protein is present, the mechanism of the reaction takes place in the following order: it starts with the de-phosphorylation of 3-phospho-2-naphthoic acid-2'-4'-dimethyl aniline by alkaline phosphatase (water is needed for the reaction). The phosphate group is released and replaced by an alcohol group from water. The electrophile 4- chloro-2-2 methylbenzenediazonium (Fast Red TR Diazonium salt) displaces the alcohol group forming the final product Red Azo dye. As its name implies, this is the final visible-red product of the reaction. In undergraduate academic experimentation of protein purification, the gel is usually run next to commercial purified samples to visualize the results and conclude whether or not purification was successful.
474:
672:, which is rarely used, based on Pubmed citations (LB), isoelectric histidine, pK matched goods buffers, etc.; in most cases the purported rationale is lower current (less heat) matched ion mobilities, which leads to longer buffer life. Borate is problematic; Borate can polymerize, or interact with cis diols such as those found in RNA. TAE has the lowest buffering capacity but provides the best resolution for larger DNA. This means a lower voltage and more time, but a better product. LB is relatively new and is ineffective in resolving fragments larger than 5 kbp; However, with its low conductivity, a much higher voltage could be used (up to 35 V/cm), which means a shorter analysis time for routine electrophoresis. As low as one base pair size difference could be resolved in 3% agarose gel with an extremely low conductivity medium (1 mM Lithium borate).
322:
pH, but running for too long can exhaust the buffering capacity of the solution. There are also limitations in determining the molecular weight by SDS-PAGE, especially when trying to find the MW of an unknown protein. Certain biological variables are difficult or impossible to minimize and can affect electrophoretic migration. Such factors include protein structure, post-translational modifications, and amino acid composition. For example, tropomyosin is an acidic protein that migrates abnormally on SDS-PAGE gels. This is because the acidic residues are repelled by the negatively charged SDS, leading to an inaccurate mass-to-charge ratio and migration. Further, different preparations of genetic material may not migrate consistently with each other, for morphological or other reasons.
103:
238:. The electric field consists of a negative charge at one end which pushes the molecules through the gel, and a positive charge at the other end that pulls the molecules through the gel. The molecules being sorted are dispensed into a well in the gel material. The gel is placed in an electrophoresis chamber, which is then connected to a power source. When the electric field is applied, the larger molecules move more slowly through the gel while the smaller molecules move faster. The different sized molecules form distinct bands on the gel.
297:(EMF) that is used to move the molecules through the gel matrix. By placing the molecules in wells in the gel and applying an electric field, the molecules will move through the matrix at different rates, determined largely by their mass when the charge-to-mass ratio (Z) of all species is uniform. However, when charges are not all uniform the electrical field generated by the electrophoresis procedure will cause the molecules to migrate differentially according to charge. Species that are net positively charged will migrate towards the
966:(SDS) that coats the proteins with a negative charge. Generally, the amount of SDS bound is relative to the size of the protein (usually 1.4g SDS per gram of protein), so that the resulting denatured proteins have an overall negative charge, and all the proteins have a similar charge-to-mass ratio. Since denatured proteins act like long rods instead of having a complex tertiary shape, the rate at which the resulting SDS coated proteins migrate in the gel is relative only to their size and not their charge or shape.
570:
388:"Most agarose gels are made with between 0.7% (good separation or resolution of large 5–10kb DNA fragments) and 2% (good resolution for small 0.2–1kb fragments) agarose dissolved in electrophoresis buffer. Up to 3% can be used for separating very tiny fragments but a vertical polyacrylamide gel is more appropriate in this case. Low percentage gels are very weak and may break when you try to lift them. High percentage gels are often brittle and do not set evenly. 1% gels are common for many applications."
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distribution), which then can be used in further products/processes (e.g. self-assembly processes). For the separation of nanoparticles within a gel, the key parameter is the ratio of the particle size to the mesh size, whereby two migration mechanisms were identified: the unrestricted mechanism, where the particle size << mesh size, and the restricted mechanism, where particle size is similar to mesh size.
220:
3247:
840:. The results can be analyzed quantitatively by visualizing the gel with UV light and a gel imaging device. The image is recorded with a computer-operated camera, and the intensity of the band or spot of interest is measured and compared against standard or markers loaded on the same gel. The measurement and analysis are mostly done with specialized software.
313:
separation of the components can lead to overlapping bands, or indistinguishable smears representing multiple unresolved components. Bands in different lanes that end up at the same distance from the top contain molecules that passed through the gel at the same speed, which usually means they are approximately the same size. There are
605:. Complexes remain—for the most part—associated and folded as they would be in the cell. One downside, however, is that complexes may not separate cleanly or predictably, as it is difficult to predict how the molecule's shape and size will affect its mobility. Addressing and solving this problem is a major aim of
888:, however, may show multiple bands, the speed of migration may depend on whether it is relaxed or supercoiled. Single-stranded DNA or RNA tends to fold up into molecules with complex shapes and migrate through the gel in a complicated manner based on their tertiary structure. Therefore, agents that disrupt the
938:
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Electrophoresis of RNA samples can be used to check for genomic DNA contamination and also for RNA degradation. RNA from eukaryotic organisms shows distinct bands of 28s and 18s rRNA, the 28s band being approximately twice as intense as the 18s band. Degraded RNA has less sharply defined bands, has a
593:
Native gels are run in non-denaturing conditions so that the analyte's natural structure is maintained. This allows the physical size of the folded or assembled complex to affect the mobility, allowing for analysis of all four levels of the biomolecular structure. For biological samples, detergents
317:
available that contain a mixture of molecules of known sizes. If such a marker was run on one lane in the gel parallel to the unknown samples, the bands observed can be compared to those of the unknown to determine their size. The distance a band travels is approximately inversely proportional to the
628:
and intrinsic charge, but also the cross-sectional area, and thus experience different electrophoretic forces dependent on the shape of the overall structure. For proteins, since they remain in the native state they may be visualized not only by general protein staining reagents but also by specific
402:
Polyacrylamide gel electrophoresis (PAGE) is used for separating proteins ranging in size from 5 to 2,000 kDa due to the uniform pore size provided by the polyacrylamide gel. Pore size is controlled by modulating the concentrations of acrylamide and bis-acrylamide powder used in creating a gel. Care
376:
to several megabases (millions of bases), the largest of which require specialized apparatus. The distance between DNA bands of different lengths is influenced by the percent agarose in the gel, with higher percentages requiring longer run times, sometimes days. Instead high percentage agarose gels
321:
There are limits to electrophoretic techniques. Since passing a current through a gel causes heating, gels may melt during electrophoresis. Electrophoresis is performed in buffer solutions to reduce pH changes due to the electric field, which is important because the charge of DNA and RNA depends on
312:
If several samples have been loaded into adjacent wells in the gel, they will run parallel in individual lanes. Depending on the number of different molecules, each lane shows the separation of the components from the original mixture as one or more distinct bands, one band per component. Incomplete
659:
Buffers in gel electrophoresis are used to provide ions that carry a current and to maintain the pH at a relatively constant value. These buffers have plenty of ions in them, which is necessary for the passage of electricity through them. Something like distilled water or benzene contains few ions,
446:
are made in 6%, 8%, 10%, 12% or 15%. Stacking gel (5%) is poured on top of the resolving gel and a gel comb (which forms the wells and defines the lanes where proteins, sample buffer, and ladders will be placed) is inserted. The percentage chosen depends on the size of the protein that one wishes
330:
The types of gel most typically used are agarose and polyacrylamide gels. Each type of gel is well-suited to different types and sizes of the analyte. Polyacrylamide gels are usually used for proteins and have very high resolving power for small fragments of DNA (5-500 bp). Agarose gels, on the
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A 1959 book on electrophoresis by Milan Bier cites references from the 1800s. However, Oliver
Smithies made significant contributions. Bier states: "The method of Smithies ... is finding wide application because of its unique separatory power." Taken in context, Bier clearly implies that Smithies'
172:
or other substances. Shorter molecules move faster and migrate farther than longer ones because shorter molecules migrate more easily through the pores of the gel. This phenomenon is called sieving. Proteins are separated by the charge in agarose because the pores of the gel are too large to sieve
48:
is placed in this buffer-filled box and an electric current is applied via the power supply to the rear. The negative terminal is at the far end (black wire), so DNA migrates toward the positively charged anode(red wire). This occurs because phosphate groups found in the DNA fragments possess a
180:
Gel electrophoresis uses a gel as an anticonvective medium or sieving medium during electrophoresis, the movement of a charged particle in an electric current. Gels suppress the thermal convection caused by the application of the electric field, and can also act as a sieving medium, slowing the
459:
potato starch makes for another non-toxic medium for protein electrophoresis. The gels are slightly more opaque than acrylamide or agarose. Non-denatured proteins can be separated according to charge and size. They are visualised using
Napthal Black or Amido Black staining. Typical starch gel
1023:
A novel application for gel electrophoresis is the separation or characterization of metal or metal oxide nanoparticles (e.g. Au, Ag, ZnO, SiO2) regarding the size, shape, or surface chemistry of the nanoparticles. The scope is to obtain a more homogeneous sample (e.g. narrower particle size
632:
A specific experiment example of an application of native gel electrophoresis is to check for enzymatic activity to verify the presence of the enzyme in the sample during protein purification. For example, for the protein alkaline phosphatase, the staining solution is a mixture of
418:
methods used polyacrylamide gels to separate DNA fragments differing by a single base-pair in length so the sequence could be read. Most modern DNA separation methods now use agarose gels, except for particularly small DNA fragments. It is currently most often used in the field of
335:(PFGE). Polyacrylamide gels are run in a vertical configuration while agarose gels are typically run horizontally in a submarine mode. They also differ in their casting methodology, as agarose sets thermally, while polyacrylamide forms in a chemical polymerization reaction.
368:. Agarose gels are easily cast and handled compared to other matrices because the gel setting is a physical rather than chemical change. Samples are also easily recovered. After the experiment is finished, the resulting gel can be stored in a plastic bag in a refrigerator.
679:
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 on a single sharp band in a process called
97:
The image above shows how small DNA fragments will migrate through agarose quickly but large size DNA fragments move more slowly during electrophoresis. The graph to the right shows the nonlinear relationship between the size of the DNA fragment and the distance
285:
and must be handled using appropriate safety precautions to avoid poisoning. Agarose is composed of long unbranched chains of uncharged carbohydrates without cross-links resulting in a gel with large pores allowing for the separation of macromolecules and
684:. Separation of the proteins by size is achieved in the lower, "resolving" region of the gel. The resolving gel typically has a much smaller pore size, which leads to a sieving effect that now determines the electrophoretic mobility of the proteins.
309:), whereas species that are net negatively charged will migrate towards the positively charged anode. Mass remains a factor in the speed with which these non-uniformly charged molecules migrate through the matrix toward their respective electrodes.
181:
passage of molecules; gels can also simply serve to maintain the finished separation so that a post electrophoresis stain can be applied. DNA gel electrophoresis is usually performed for analytical purposes, often after amplification of DNA via
954:, unlike nucleic acids, can have varying charges and complex shapes, therefore they may not migrate into the polyacrylamide gel at similar rates, or all when placing a negative to positive EMF on the sample. Proteins, therefore, are usually
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Agarose gels do not have a uniform pore size, but are optimal for electrophoresis of proteins that are larger than 200 kDa. Agarose gel electrophoresis can also be used for the separation of DNA fragments ranging from 50
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Barasinski, Matthäus; Garnweitner, Georg (12 February 2020). "Restricted and
Unrestricted Migration Mechanisms of Silica Nanoparticles in Agarose Gels and Their Utilization for the Separation of Binary Mixtures".
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to identify or probe in the sample. The smaller the known weight, the higher the percentage that should be used. Changes in the buffer system of the gel can help to further resolve proteins of very small sizes.
331:
other hand, have lower resolving power for DNA but have a greater range of separation, and are therefore used for DNA fragments of usually 50–20,000 bp in size, but the resolution of over 6 Mb is possible with
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Depending on the type of analysis being performed, other techniques are often implemented in conjunction with the results of gel electrophoresis, providing a wide range of field-specific applications.
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Denaturing conditions are necessary for proper estimation of molecular weight of RNA. RNA is able to form more intramolecular interactions than DNA which may result in change of its
1995:
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TTGE profiles representing the bifidobacterial diversity of fecal samples from two healthy volunteers (A and B) before and after AMC (Oral
Amoxicillin-Clavulanic Acid) treatment
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is a process that enables the sorting of molecules based on charge, size, or shape. Using an electric field, molecules (such as DNA) can be made to move through a gel made of
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915:" page for an example of a polyacrylamide DNA sequencing gel. Characterization through ligand interaction of nucleic acids or fragments may be performed by mobility shift
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logarithm of the size of the molecule (alternatively, this can be stated as the distance traveled is inversely proportional to the log of samples's molecular weight).
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In the case of nucleic acids, the direction of migration, from negative to positive electrodes, is due to the naturally occurring negative charge carried by their
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Gel electrophoresis is a process where an electric current is applied to DNA samples creating fragments that can be used for comparison between DNA samples.
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Double-stranded DNA fragments naturally behave as long rods, so their migration through the gel is relative to their size or, for cyclic fragments, their
766:. The gel will then be physically cut, and the protein complexes extracted from each portion separately. Each extract may then be analysed, such as by
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gels are run under conditions that disrupt the natural structure of the analyte, causing it to unfold into a linear chain. Thus, the mobility of each
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281:), the preferred matrix is purified agarose. In both cases, the gel forms a solid, yet porous matrix. Acrylamide, in contrast to polyacrylamide, is a
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which is not ideal for the use in electrophoresis. There are a number of buffers used for electrophoresis. The most common being, for nucleic acids
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to separate a mixed population of DNA and RNA fragments by length, to estimate the size of DNA and RNA fragments or to separate proteins by charge.
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dye. Other methods may also be used to visualize the separation of the mixture's components on the gel. If the molecules to be separated contain
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whose composition and porosity are chosen based on the specific weight and composition of the target to be analyzed. When separating
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Smisek, David L.; Hoagland, David A. (1989). "Agarose gel electrophoresis of high molecular weight, synthetic polyelectrolytes".
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Electrophoresis of
Proteins in Polyacrylamide and Starch Gels: Laboratory Techniques in Biochemistry and Molecular Biology
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depends only on its linear length and its mass-to-charge ratio. Thus, the secondary, tertiary, and quaternary levels of
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245:" in this instance refers to the matrix used to contain, then separate the target molecules. In most cases, the gel is a
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system. Gels are then commonly labelled for presentation and scientific records on the popular figure-creation website,
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negative charge which is repelled by the negatively charged cathode and are attracted to the positively charged anode.
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must be used when creating this type of gel, as acrylamide is a potent neurotoxin in its liquid and powdered forms.
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1976:"Enhanced full-length transcription of Sindbis virus RNA by effective denaturation with methylmercury hydroxide"
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hydroxide was often used in denaturing RNA electrophoresis, but it may be method of choice for some samples.
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Minde, David P.; Maurice, Madelon M.; RĂĽdiger, Stefan G. D. (3 October 2012). Uversky, Vladimir N. (ed.).
2464:"The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis"
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1835:"Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults"
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2070:"Length-independent separation of DNA restriction fragments in two-dimensional gel electrophoresis"
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778:. This can provide a great deal of information about the identities of the proteins in a complex.
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2017:
Fromin N; Hamelin J; Tarnawski S; Roesti D; Jourdain-Miserez K; Forestier N; et al. (2002).
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Hanauer, Matthias; Pierrat, Sebastien; Zins, Inga; Lotz, Alexander; Sönnichsen, Carsten (2007).
39:
1287:"Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104"
519:, a method called reducing PAGE. Reducing conditions are usually maintained by the addition of
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are the most often used denaturing agents to disrupt RNA structure. Originally, highly toxic
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2614:"Determining Biophysical Protein Stability in Lysates by a Fast Proteolysis Assay, FASTpp"
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to separate proteins by charge or size (IEF agarose, essentially size independent) and in
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process. For full denaturation of proteins, it is also necessary to reduce the covalent
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Estimation of the size of DNA molecules following restriction enzyme digestion, e.g. in
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Denaturing gel electrophoresis is used in the DNA and RNA banding pattern-based methods
185:(PCR), but may be used as a preparative technique prior to use of other methods such as
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2019:"Statistical analysis of denaturing gel electrophoresis (DGE) fingerprinting patterns"
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900:, are used to denature the nucleic acids and cause them to behave as long rods again.
527:. For a general analysis of protein samples, reducing PAGE is the most common form of
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947:– The indicated proteins are present in different concentrations in the two samples.
647:. However, native PAGE is also used to scan genes (DNA) for unknown mutations as in
2950:
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2101:
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Wilson and Walker's principles and techniques of biochemistry and molecular biology
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1984 – pulsed-field gel electrophoresis enables separation of large DNA molecules (
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are usually analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (
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2322:"Separation of Nanoparticles by Gel Electrophoresis According to Size and Shape"
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134:
1048:
1950 – introduction of "zone electrophoresis" (Tiselius); paper electrophoresis
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1708:
1581:. Vol. 1 (3rd ed.). Cold Spring Harbor Laboratory. p. 5.2–5.3.
1577:
Tom
Maniatis; E. F. Fritsch; Joseph Sambrook (1982). "Chapter 5, protocol 1".
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membrane to be probed with antibodies and corresponding markers, such as in a
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2233:"History and principles of conductive media for standard DNA electrophoresis"
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Unlike denaturing methods, native gel electrophoresis does not use a charged
1646:
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1330:(in Spanish). Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory Press.
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After separation, an additional separation method may then be used, such as
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2018:
1935:"Synthesis of full length cDNAs from four partially purified oviduct mRNAs"
1868:
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149:, etc.) and their fragments, based on their size and charge. It is used in
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of the same protein into separate bands. These can be transferred onto a
424:
2310:
Troubleshooting DNA agarose gel electrophoresis. Focus 19:3 p.66 (1997).
1623:
1070:); accurate control of parameters such as pore size and stability; and (
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After the electrophoresis is complete, the molecules in the gel can be
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2132:"Detection of glucose-6-phosphate dehydrogenase in malarial parasites"
1850:
1401:. Cambridge, United Kingdom New York, NY: Cambridge University Press.
1285:
Kryndushkin DS; Alexandrov IM; Ter-Avanesyan MD; Kushnirov VV (2003).
173:
proteins. Gel electrophoresis can also be used for the separation of
1052:
1012:
1008:
2413:"Electrophoretic separation of polyoma virus DNA from host cell DNA"
2208:
fundamental laboratory approaches for biochemistry and biotechnology
937:
857:
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and protein analysis, often used to separate different proteins or
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are disrupted, leaving only the primary structure to be analyzed.
342:
101:
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1884:"A thin-layer starch gel method for enzyme typing of bloodstains"
1509:
1498:"Agarose gel electrophoresis for the separation of DNA fragments"
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Characterization through ligand interaction may be performed by
539:
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432:
347:
Inserting the gel comb in an agarose gel electrophoresis chamber
3003:
2722:
2685:, from the University of Utah's Genetic Science Learning Center
2206:
Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2009).
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smeared appearance, and the intensity ratio is less than 2:1.
908:
904:
262:
258:
242:
142:
138:
269:) the gel is usually composed of different concentrations of
168:
to move the negatively charged molecules through a matrix of
2557:
561:(TGGE) and denaturing gradient gel electrophoresis (DGGE).
911:
is usually done by agarose gel electrophoresis. See the "
694:
Gel electrophoresis of nucleic acids § Visualization
2183:
Fundamental
Approaches to Biochemistry and Biotechnology
675:
Most SDS-PAGE protein separations are performed using a
2709:
Step by step photos of running a gel and extracting DNA
594:
are used only to the extent that they are necessary to
2683:
Biotechniques
Laboratory electrophoresis demonstration
747:
698:
Gel electrophoresis of proteins § Visualization
164:
Nucleic acid molecules are separated by applying an
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3050:
2974:
2938:
2910:
2867:
2761:
1933:Buell GN; Wickens MP; Payvar F; Schimke RT (1978).
1542:"Molecular Weight Determination by SDS-PAGE, Rev B"
668:(TBE). Many other buffers have been proposed, e.g.
69:
64:
54:
2591:Electrophoresis: theory, methods, and applications
2283:
1077:1965 – introduction of free-flow electrophoresis (
706:to make them visible. DNA may be visualized using
499:in the buffer, while proteins are denatured using
27:Method for separation and analysis of biomolecules
2376:(9). American Chemical Society (ACS): 5157–5166.
1610:(5). American Chemical Society (ACS): 2270–2277.
1465:Biochemical techniques : theory and practice
1434:(in Estonian). San Francisco: Benjamin Cummings.
1150:1981 – introduction of capillary electrophoresis
2689:Discontinuous native protein gel electrophoresis
2624:(10). Public Library of Science (PLoS): e46147.
301:which is negatively charged (because this is an
1828:
1826:
1125:1972 – agarose gels with ethidium bromide stain
495:Nucleic acids are often denatured by including
1496:Lee PY; Costumbrado J; Hsu CY; Kim YH (2012).
1007:and determination of structural features like
808:Separation of restricted genomic DNA prior to
616:agent. The molecules being separated (usually
3015:
2734:
980:, by preparative native gel electrophoresis (
718:light, while protein may be visualised using
8:
2704:Animation of gel analysis of DNA restriction
1709:"Agarose gel electrophoresis (basic method)"
1328:Molecular cloning : a laboratory manual
32:
133:is a method for separation and analysis of
3022:
3008:
3000:
2741:
2727:
2719:
2290:(5th ed.). WH Freeman: New York, NY.
2185:. Bethesda, Md: Fitzgerald Science Press.
38:
2655:
2637:
2479:
1950:
1858:
1517:
1467:. Prospect Heights, Ill: Waveland Press.
1302:
639:gel electrophoresis is typically used in
3143:Temperature gradient gel electrophoresis
1359:
1357:
1355:
559:temperature gradient gel electrophoresis
472:
218:
86:Temperature gradient gel electrophoresis
2282:Lodish H; Berk A; Matsudaira P (2004).
1579:Molecular Cloning - A Laboratory Manual
1368:(in Estonian). New York: W.H. Freeman.
1277:
677:"discontinuous" (or DISC) buffer system
649:single-strand conformation polymorphism
357:Agarose gels are made from the natural
2984:Photoactivated localization microscopy
2902:Protein–protein interaction prediction
1167:2004 – introduction of a standardized
31:
1558:from the original on 17 November 2021
1066:gels; discontinuous electrophoresis (
118:Electric current applied to the gel.
112:Isolation and amplification of DNA.
7:
3246:
3174:Gel electrophoresis of nucleic acids
3103:Electrophoretic mobility shift assay
1801:. Amsterdam: North-Holland Pub. Co.
1719:from the original on 11 October 2018
1689:from the original on 2 February 2022
1215:Electrophoretic mobility shift assay
1033:1930s – first reports of the use of
853:Gel electrophoresis of nucleic acids
742:can be taken of gels, often using a
3169:DNA separation by silica adsorption
3148:Two-dimensional gel electrophoresis
2859:Freeze-fracture electron microscopy
2370:The Journal of Physical Chemistry C
2210:. Hoboken, NJ: Wiley. p. 161.
1240:Two-dimensional gel electrophoresis
710:which, when intercalated into DNA,
82:Two-dimensional gel electrophoresis
44:Gel electrophoresis apparatus – an
3133:Polyacrylamide gel electrophoresis
2560:. De Gruyter, ISBN 9783110761627.
398:Polyacrylamide gel electrophoresis
25:
2714:A typical method from wikiversity
2535:from the original on 11 June 2022
2443:from the original on 11 June 2022
2263:from the original on 11 June 2022
2111:from the original on 11 June 2022
2049:from the original on 11 June 2022
1998:from the original on 11 June 2022
1914:from the original on 11 June 2022
1882:Wraxall BG; Culliford BJ (1968).
1778:from the original on 11 June 2022
865:product compared to a DNA ladder.
575:Glucose-6-Phosphate Dehydrogenase
573:Specific enzyme-linked staining:
121:DNA bands are separated by size.
3245:
3234:
3233:
3138:Pulsed-field gel electrophoresis
2839:Isothermal titration calorimetry
2819:Dual-polarization interferometry
2505:"The gel electrophoresis of DNA"
2162:from the original on 6 July 2023
2130:Hempelmann E; Wilson RJ (1981).
2035:10.1046/j.1462-2920.2002.00358.x
1432:Modern experimental biochemistry
1230:Pulsed field gel electrophoresis
333:pulsed field gel electrophoresis
223:Overview of gel electrophoresis.
3179:Gel electrophoresis of proteins
3128:Moving-boundary electrophoresis
3068:Capillary electrochromatography
2593:. Academic Press. p. 225.
1651:Current Protocols in Immunology
1039:moving-boundary electrophoresis
933:Gel electrophoresis of proteins
820:Gel electrophoresis is used in
624:) therefore differ not only in
383:field inversion electrophoresis
3083:Difference gel electrophoresis
2694:Drinking straw electrophoresis
2068:Fischer SG; Lerman LS (1979).
1136:, then SDS gel electrophoresis
460:concentrations are 5% to 10%.
293:Electrophoresis refers to the
205:for further characterization.
1:
3184:Serum protein electrophoresis
3088:Discontinuous electrophoresis
2829:Chromatin immunoprecipitation
2481:10.1016/S0021-9258(18)94333-4
1952:10.1016/S0021-9258(17)38097-3
1900:10.1016/s0015-7368(68)70449-7
1653:. Chapter 10: 10.4.1–10.4.8.
1647:"Agarose gel electrophoresis"
903:Gel electrophoresis of large
738:can be recorded of the gel.
315:molecular weight size markers
115:DNA added to the gel wells.
2892:Protein structural alignment
2877:Protein structure prediction
2639:10.1371/journal.pone.0046147
2521:10.1016/0005-2787(72)90426-1
2429:10.1016/0042-6822(66)90029-8
2181:Ninfa AJ, Ballou DP (1998).
2148:10.1016/0166-6851(81)90100-6
2086:10.1016/0092-8674(79)90200-9
1974:Schelp C, Kaaden OR (1989).
1659:10.1002/0471142735.im1004s02
1122:using a stacking gel and SDS
798:products, e.g. in molecular
379:pulsed field electrophoresis
3063:Agarose gel electrophoresis
2976:Super-resolution microscopy
2882:Protein function prediction
2810:Peptide mass fingerprinting
2805:Protein immunoprecipitation
2699:How to run a DNA or RNA gel
1645:Voytas, Daniel (May 2001).
1128:1975 – 2-dimensional gels (
1118:separated 28 components of
1055:gels, mediocre separation (
768:peptide mass fingerprinting
353:Agarose gel electrophoresis
3322:
3042:History of electrophoresis
2462:Weber K; Osborn M (1969).
2231:Brody JR; Kern SE (2004).
1210:History of electrophoresis
1199:method is an improvement.
978:native gel electrophoresis
930:
850:
772:de novo peptide sequencing
691:
395:
350:
212:
18:Native gel electrophoresis
3301:Polymerase chain reaction
3229:
3221:Electrophoresis (journal)
3073:Capillary electrophoresis
3037:
2834:Surface plasmon resonance
2824:Microscale thermophoresis
2814:Protein mass spectrometry
2776:Green fluorescent protein
1326:Sambrook, Joseph (2001).
1265:Free-flow electrophoresis
1260:Fast parallel proteolysis
1235:Nonlinear frictiophoresis
1037:for gel electrophoresis;
1001:capillary electrophoresis
503:, usually as part of the
183:polymerase chain reaction
74:Capillary electrophoresis
37:
3058:Affinity electrophoresis
2854:Cryo-electron microscopy
2503:Aaij C; Borst P (1972).
2382:10.1021/acs.jpcc.9b10644
2249:10.1016/j.ab.2004.05.054
997:affinity electrophoresis
917:affinity electrophoresis
913:chain termination method
724:Coomassie brilliant blue
629:enzyme-linked staining.
536:electrophoretic mobility
288:macromolecular complexes
124:DNA bands are stained.
2887:Protein–protein docking
2800:Protein electrophoresis
1091:1969 – introduction of
1062:1959 – introduction of
1051:1955 – introduction of
884:. Circular DNA such as
607:preparative native PAGE
529:protein electrophoresis
2786:Protein immunostaining
2286:Molecular Cell Biology
1430:Boyer, Rodney (2000).
1397:Wilson, Keith (2018).
1304:10.1074/jbc.M307996200
1152:(Jorgenson and Lukacs)
964:sodium dodecyl sulfate
948:
866:
804:genetic fingerprinting
590:
501:sodium dodecyl sulfate
490:biomolecular structure
478:
348:
224:
127:
99:
3291:Laboratory techniques
3113:Immunoelectrophoresis
3098:Electrochromatography
2844:X-ray crystallography
2566:10.1515/9783110761641
2136:Mol Biochem Parasitol
1797:Gordon, A.H. (1969).
1364:Berg, Jeremy (2002).
1072:Raymond and Weintraub
1003:as for estimation of
958:in the presence of a
940:
860:
812:, or of RNA prior to
754:Downstream processing
692:Further information:
583:Plasmodium falciparum
572:
511:that stabilize their
476:
377:should be run with a
346:
222:
105:
96:
3259:Analytical Chemistry
3205:Isoelectric focusing
2771:Protein purification
2589:Bier, Milan (1959).
2509:Biochim Biophys Acta
1756:10.1038/nprot.2006.4
1713:Biological Protocols
1463:Robyt, John (1990).
1225:Isoelectric focusing
1134:isoelectric focusing
1084:1966 – first use of
861:An agarose gel of a
760:isoelectric focusing
521:beta-mercaptoethanol
517:quaternary structure
3200:Electrical mobility
3108:Gel electrophoresis
2796:Gel electrophoresis
2630:2012PLoSO...746147M
2554:Michov, B. (2022).
2338:2007NanoL...7.2881H
1833:Smithies O (1955).
1738:Schägger H (2006).
1624:10.1021/ma00195a048
1616:1989MaMol..22.2270S
1169:polymerization time
986:2-D electrophoresis
789:restriction mapping
730:, for example in a
410:techniques such as
295:electromotive force
247:crosslinked polymer
131:Gel electrophoresis
34:
33:Gel electrophoresis
2939:Display techniques
2791:Protein sequencing
2411:Thorne HV (1966).
1888:J Forensic Sci Soc
1740:"Tricine-SDS-PAGE"
1095:agents especially
1068:Ornstein and Davis
949:
882:radius of gyration
867:
591:
479:
349:
225:
151:clinical chemistry
128:
109:DNA is extracted.
100:
3286:Molecular biology
3268:
3267:
3078:Dielectrophoresis
2997:
2996:
2946:Bacterial display
2346:10.1021/nl071615y
2297:978-0-7167-4366-8
2023:Environ Microbiol
1851:10.1042/bj0610629
1808:978-0-7204-4202-1
1474:978-0-88133-556-9
1441:978-0-8053-3111-0
1408:978-1-316-61476-1
1375:978-0-7167-4955-4
1337:978-0-87969-576-7
1005:binding constants
999:in agarose or by
826:molecular biology
814:Northern transfer
810:Southern transfer
800:genetic diagnosis
662:Tris/Acetate/EDTA
203:Southern blotting
187:mass spectrometry
159:molecular biology
135:biomacromolecules
91:
90:
16:(Redirected from
3313:
3249:
3248:
3237:
3236:
3123:Isotachophoresis
3024:
3017:
3010:
3001:
2961:Ribosome display
2897:Protein ontology
2743:
2736:
2729:
2720:
2670:
2669:
2659:
2641:
2609:
2603:
2602:
2586:
2580:
2579:
2551:
2545:
2544:
2542:
2540:
2500:
2494:
2493:
2483:
2459:
2453:
2452:
2450:
2448:
2408:
2402:
2401:
2364:
2358:
2357:
2332:(9): 2881–2885.
2317:
2311:
2308:
2302:
2301:
2289:
2279:
2273:
2272:
2270:
2268:
2228:
2222:
2221:
2203:
2197:
2196:
2178:
2172:
2171:
2169:
2167:
2142:(3–4): 197–204.
2127:
2121:
2120:
2118:
2116:
2110:
2065:
2059:
2058:
2056:
2054:
2014:
2008:
2007:
2005:
2003:
1971:
1965:
1964:
1954:
1930:
1924:
1923:
1921:
1919:
1879:
1873:
1872:
1862:
1830:
1821:
1820:
1794:
1788:
1787:
1785:
1783:
1735:
1729:
1728:
1726:
1724:
1705:
1699:
1698:
1696:
1694:
1642:
1636:
1635:
1599:
1593:
1592:
1574:
1568:
1567:
1565:
1563:
1557:
1546:
1538:
1532:
1531:
1521:
1493:
1487:
1486:
1460:
1454:
1453:
1427:
1421:
1420:
1394:
1388:
1387:
1361:
1350:
1349:
1323:
1317:
1316:
1306:
1297:(49): 49636–43.
1282:
1182:, in particular
1011:content through
894:sodium hydroxide
776:in-gel digestion
708:ethidium bromide
682:isotachophoresis
666:Tris/Borate/EDTA
267:oligonucleotides
65:Other techniques
42:
35:
21:
3321:
3320:
3316:
3315:
3314:
3312:
3311:
3310:
3296:Electrophoresis
3281:Protein methods
3271:
3270:
3269:
3264:
3225:
3209:
3188:
3152:
3093:Electroblotting
3046:
3033:
3031:Electrophoresis
3028:
2998:
2993:
2970:
2934:
2930:Secretion assay
2906:
2863:
2757:
2747:
2679:
2674:
2673:
2611:
2610:
2606:
2588:
2587:
2583:
2576:
2553:
2552:
2548:
2538:
2536:
2502:
2501:
2497:
2474:(16): 4406–12.
2461:
2460:
2456:
2446:
2444:
2410:
2409:
2405:
2366:
2365:
2361:
2319:
2318:
2314:
2309:
2305:
2298:
2281:
2280:
2276:
2266:
2264:
2230:
2229:
2225:
2218:
2205:
2204:
2200:
2193:
2180:
2179:
2175:
2165:
2163:
2129:
2128:
2124:
2114:
2112:
2108:
2067:
2066:
2062:
2052:
2050:
2016:
2015:
2011:
2001:
1999:
1973:
1972:
1968:
1932:
1931:
1927:
1917:
1915:
1881:
1880:
1876:
1832:
1831:
1824:
1809:
1796:
1795:
1791:
1781:
1779:
1737:
1736:
1732:
1722:
1720:
1707:
1706:
1702:
1692:
1690:
1644:
1643:
1639:
1601:
1600:
1596:
1589:
1576:
1575:
1571:
1561:
1559:
1555:
1549:www.bio-rad.com
1544:
1540:
1539:
1535:
1495:
1494:
1490:
1475:
1462:
1461:
1457:
1442:
1429:
1428:
1424:
1409:
1396:
1395:
1391:
1376:
1363:
1362:
1353:
1338:
1325:
1324:
1320:
1284:
1283:
1279:
1274:
1269:
1205:
1188:electrophoresis
1171:for acrylamide
1030:
1021:
993:electroblotting
944:autoradiography
935:
929:
855:
849:
784:
756:
700:
690:
657:
599:lipid membranes
588:Red blood cells
567:
509:disulfide bonds
471:
466:
453:
400:
394:
364:extracted from
355:
341:
328:
228:Electrophoresis
217:
215:Electrophoresis
211:
84:
80:
76:
59:Electrophoresis
50:
28:
23:
22:
15:
12:
11:
5:
3319:
3317:
3309:
3308:
3303:
3298:
3293:
3288:
3283:
3273:
3272:
3266:
3265:
3263:
3262:
3255:
3243:
3230:
3227:
3226:
3224:
3223:
3217:
3215:
3211:
3210:
3208:
3207:
3202:
3196:
3194:
3190:
3189:
3187:
3186:
3181:
3176:
3171:
3166:
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3154:
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3151:
3150:
3145:
3140:
3135:
3130:
3125:
3120:
3115:
3110:
3105:
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3095:
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3085:
3080:
3075:
3070:
3065:
3060:
3054:
3052:
3048:
3047:
3045:
3044:
3038:
3035:
3034:
3029:
3027:
3026:
3019:
3012:
3004:
2995:
2994:
2992:
2991:
2986:
2980:
2978:
2972:
2971:
2969:
2968:
2963:
2958:
2953:
2948:
2942:
2940:
2936:
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2927:
2922:
2916:
2914:
2908:
2907:
2905:
2904:
2899:
2894:
2889:
2884:
2879:
2873:
2871:
2869:Bioinformatics
2865:
2864:
2862:
2861:
2856:
2851:
2846:
2841:
2836:
2831:
2826:
2821:
2816:
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2793:
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2783:
2778:
2773:
2767:
2765:
2759:
2758:
2748:
2746:
2745:
2738:
2731:
2723:
2717:
2716:
2711:
2706:
2701:
2696:
2691:
2686:
2678:
2677:External links
2675:
2672:
2671:
2604:
2581:
2574:
2546:
2515:(2): 192–200.
2495:
2454:
2403:
2359:
2312:
2303:
2296:
2274:
2223:
2217:978-0470087664
2216:
2198:
2191:
2173:
2122:
2080:(1): 191–200.
2060:
2029:(11): 634–43.
2009:
1986:(3): 297–302.
1966:
1945:(7): 2471–82.
1925:
1874:
1822:
1807:
1789:
1730:
1700:
1637:
1604:Macromolecules
1594:
1588:978-0879691363
1587:
1569:
1533:
1488:
1473:
1455:
1440:
1422:
1407:
1389:
1374:
1351:
1336:
1318:
1276:
1275:
1273:
1270:
1268:
1267:
1262:
1257:
1252:
1247:
1242:
1237:
1232:
1227:
1222:
1220:Gel extraction
1217:
1212:
1206:
1204:
1201:
1196:
1195:
1180:gel properties
1165:
1154:
1148:
1137:
1126:
1123:
1112:
1099:separation of
1089:
1082:
1075:
1060:
1049:
1046:
1029:
1026:
1020:
1017:
931:Main article:
928:
925:
890:hydrogen bonds
851:Main article:
848:
845:
818:
817:
806:
792:
791:of cloned DNA.
783:
780:
755:
752:
732:DNA sequencing
689:
686:
670:lithium borate
656:
653:
626:molecular mass
566:
563:
525:dithiothreitol
470:
467:
465:
464:Gel conditions
462:
452:
449:
444:resolving gels
429:nitrocellulose
408:DNA sequencing
396:Main article:
393:
392:Polyacrylamide
390:
359:polysaccharide
351:Main article:
340:
337:
327:
324:
236:polyacrylamide
210:
209:Physical basis
207:
199:DNA sequencing
166:electric field
126:
125:
122:
119:
116:
113:
110:
89:
88:
71:
67:
66:
62:
61:
56:
55:Classification
52:
51:
43:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
3318:
3307:
3304:
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3299:
3297:
3294:
3292:
3289:
3287:
3284:
3282:
3279:
3278:
3276:
3261:
3260:
3256:
3254:
3253:
3244:
3242:
3241:
3232:
3231:
3228:
3222:
3219:
3218:
3216:
3212:
3206:
3203:
3201:
3198:
3197:
3195:
3191:
3185:
3182:
3180:
3177:
3175:
3172:
3170:
3167:
3165:
3164:DNA laddering
3162:
3161:
3159:
3155:
3149:
3146:
3144:
3141:
3139:
3136:
3134:
3131:
3129:
3126:
3124:
3121:
3119:
3118:Iontophoresis
3116:
3114:
3111:
3109:
3106:
3104:
3101:
3099:
3096:
3094:
3091:
3089:
3086:
3084:
3081:
3079:
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3059:
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3025:
3020:
3018:
3013:
3011:
3006:
3005:
3002:
2990:
2987:
2985:
2982:
2981:
2979:
2977:
2973:
2967:
2966:Yeast display
2964:
2962:
2959:
2957:
2956:Phage display
2954:
2952:
2949:
2947:
2944:
2943:
2941:
2937:
2931:
2928:
2926:
2925:Protein assay
2923:
2921:
2918:
2917:
2915:
2913:
2909:
2903:
2900:
2898:
2895:
2893:
2890:
2888:
2885:
2883:
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2878:
2875:
2874:
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2707:
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2690:
2687:
2684:
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2013:
2010:
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1967:
1962:
1958:
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1944:
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1878:
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1845:(4): 629–41.
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1211:
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1189:
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1184:gel stability
1181:
1177:
1174:
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1166:
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1019:Nanoparticles
1018:
1016:
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1002:
998:
994:
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847:Nucleic acids
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844:
841:
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831:
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823:
815:
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805:
801:
797:
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736:autoradiogram
733:
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728:radioactivity
725:
721:
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713:
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688:Visualization
687:
685:
683:
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673:
671:
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623:
622:nucleic acids
619:
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589:
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584:
579:
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552:methylmercury
549:
545:
541:
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532:
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367:
363:
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323:
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316:
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307:galvanic cell
304:
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296:
291:
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284:
280:
276:
272:
268:
264:
260:
256:
255:nucleic acids
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229:
221:
216:
208:
206:
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196:
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188:
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175:nanoparticles
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111:
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95:
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83:
79:
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72:
68:
63:
60:
57:
53:
47:
41:
36:
30:
19:
3257:
3250:
3238:
3157:Applications
3107:
2951:mRNA display
2920:Enzyme assay
2795:
2781:Western blot
2763:Experimental
2621:
2617:
2607:
2590:
2584:
2556:
2549:
2537:. Retrieved
2512:
2508:
2498:
2471:
2467:
2457:
2445:. Retrieved
2423:(2): 234–9.
2420:
2416:
2406:
2373:
2369:
2362:
2329:
2326:Nano Letters
2325:
2315:
2306:
2285:
2277:
2265:. Retrieved
2240:
2237:Anal Biochem
2236:
2226:
2207:
2201:
2182:
2176:
2164:. Retrieved
2139:
2135:
2125:
2113:. Retrieved
2077:
2073:
2063:
2051:. Retrieved
2026:
2022:
2012:
2000:. Retrieved
1983:
1979:
1969:
1942:
1938:
1928:
1916:. Retrieved
1891:
1887:
1877:
1842:
1838:
1798:
1792:
1780:. Retrieved
1750:(1): 16–22.
1747:
1743:
1733:
1721:. Retrieved
1712:
1703:
1691:. Retrieved
1650:
1640:
1607:
1603:
1597:
1578:
1572:
1560:. Retrieved
1548:
1536:
1510:10.3791/3923
1501:
1491:
1464:
1458:
1431:
1425:
1398:
1392:
1366:Biochemistry
1365:
1327:
1321:
1294:
1290:
1280:
1197:
1178:to optimize
1022:
990:
968:
950:
941:
921:
902:
879:
868:
842:
838:biochemistry
834:microbiology
819:
794:Analysis of
782:Applications
757:
720:silver stain
701:
674:
658:
635:
631:
611:
592:
581:
556:
533:
494:
480:
454:
441:
437:western blot
406:Traditional
405:
401:
387:
370:
356:
329:
326:Types of gel
320:
311:
305:rather than
303:electrolytic
292:
275:cross-linker
240:
226:
179:
163:
155:biochemistry
130:
129:
29:
2989:Vertico SMI
2849:Protein NMR
2468:J Biol Chem
2243:(1): 1–13.
1939:J Biol Chem
1894:(2): 81–2.
1291:J Biol Chem
740:Photographs
716:ultraviolet
645:metallomics
46:agarose gel
3275:Categories
3051:Techniques
1980:Acta Virol
1744:Nat Protoc
1272:References
1255:Zymography
1192:Kastenholz
1141:sequencing
1093:denaturing
1064:acrylamide
892:, such as
877:backbone.
641:proteomics
614:denaturing
578:isoenzymes
482:Denaturing
469:Denaturing
457:hydrolysed
455:Partially
442:Typically
421:immunology
381:(PFE), or
283:neurotoxin
271:acrylamide
241:The term "
213:See also:
2648:1932-6203
2398:213566317
2390:1932-7447
1839:Biochem J
1772:209529082
1667:1934-368X
1632:0024-9297
1502:J Vis Exp
1417:998750377
1250:QPNC-PAGE
1186:, during
1176:solutions
1130:O’Farrell
1103:subunit (
1015:binding.
984:), or by
982:QPNC-PAGE
960:detergent
956:denatured
942:SDS-PAGE
898:formamide
875:phosphate
822:forensics
712:fluoresce
586:infected
374:base pair
253:or small
98:migrated.
3240:Category
3214:Journals
2756:of study
2750:Proteins
2666:23056252
2618:PLOS ONE
2539:23 March
2533:Archived
2447:23 March
2441:Archived
2417:Virology
2354:17718532
2267:23 March
2261:Archived
2257:15351274
2166:23 March
2160:Archived
2115:23 March
2106:Archived
2053:23 March
2047:Archived
2043:12460271
2002:23 March
1996:Archived
1918:23 March
1912:Archived
1869:13276348
1782:23 March
1776:Archived
1764:17406207
1723:23 March
1717:Archived
1687:Archived
1683:39623776
1675:18432695
1562:23 March
1553:Archived
1528:22546956
1483:22549624
1450:44493241
1384:48055706
1346:45015638
1313:14507919
1203:See also
1158:Schwartz
1120:T4 phage
1057:Smithies
1043:Tiselius
974:SDS-PAGE
970:Proteins
962:such as
952:Proteins
927:Proteins
886:plasmids
830:genetics
764:SDS-PAGE
734:gel, an
618:proteins
513:tertiary
505:SDS-PAGE
425:isoforms
362:polymers
251:proteins
147:proteins
78:SDS-PAGE
3252:Commons
2754:methods
2657:3463568
2626:Bibcode
2599:1175404
2529:5063906
2490:5806584
2437:4287545
2334:Bibcode
2156:7012616
2102:9369012
1992:2570517
1908:5738223
1860:1215845
1693:1 March
1612:Bibcode
1519:4846332
1245:SDD-AGE
1139:1977 –
1114:1970 –
1101:protein
1035:sucrose
1028:History
744:Gel Doc
704:stained
664:(TAE),
655:Buffers
601:in the
548:glyoxal
366:seaweed
339:Agarose
299:cathode
232:agarose
195:cloning
193:, PCR,
170:agarose
70:Related
3193:Theory
2752:: key
2664:
2654:
2646:
2597:
2572:
2527:
2488:
2435:
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1990:
1961:632280
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1481:
1471:
1448:
1438:
1415:
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1382:
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1344:
1334:
1311:
1162:Cantor
1145:Sanger
1143:gels (
1116:Lämmli
1109:Osborn
1079:Hannig
1053:starch
1013:lectin
1009:glycan
995:or by
976:), by
774:after
748:SciUGo
714:under
696:, and
637:Native
565:Native
451:Starch
416:Sanger
273:and a
2912:Assay
2394:S2CID
2109:(PDF)
2098:S2CID
1817:21766
1768:S2CID
1679:S2CID
1556:(PDF)
1545:(PDF)
1105:Weber
871:sugar
279:bases
265:, or
201:, or
3306:Gels
2662:PMID
2644:ISSN
2595:OCLC
2570:ISBN
2541:2022
2525:PMID
2486:PMID
2449:2022
2433:PMID
2386:ISSN
2350:PMID
2292:ISBN
2269:2022
2253:PMID
2212:ISBN
2187:ISBN
2168:2022
2152:PMID
2117:2022
2090:PMID
2074:Cell
2055:2022
2039:PMID
2004:2022
1988:PMID
1957:PMID
1920:2022
1904:PMID
1865:PMID
1813:OCLC
1803:ISBN
1784:2022
1760:PMID
1725:2022
1695:2023
1671:PMID
1663:ISSN
1628:ISSN
1583:ISBN
1564:2022
1524:PMID
1479:OCLC
1469:ISBN
1446:OCLC
1436:ISBN
1413:OCLC
1403:ISBN
1380:OCLC
1370:ISBN
1342:OCLC
1332:ISBN
1309:PMID
1160:and
1107:and
1088:gels
1086:agar
836:and
643:and
603:cell
596:lyse
546:and
544:DMSO
540:Urea
515:and
497:urea
433:PVDF
191:RFLP
157:and
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2634:doi
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2082:doi
2031:doi
1947:doi
1943:253
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1855:PMC
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1506:doi
1299:doi
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1173:gel
1132:);
1097:SDS
909:RNA
907:or
905:DNA
896:or
863:PCR
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796:PCR
770:or
762:or
722:or
620:or
580:in
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259:DNA
243:gel
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