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  2. SDS-PAGE - Wikipedia

    en.wikipedia.org/wiki/SDS-PAGE

    SDS-PAGE is the most widely used method for gel electrophoretic separation of proteins. Two-dimensional gel electrophoresis sequentially combines isoelectric focusing or BAC-PAGE with a SDS-PAGE. [52] [53] Native PAGE is used if native protein folding is to be maintained. For separation of membrane proteins, BAC-PAGE or CTAB-PAGE may be used as ...

  3. Polyacrylamide gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Polyacrylamide_gel...

    Picture of an SDS-PAGE. The molecular markers (ladder) are in the left lane. Polyacrylamide gel electrophoresis (PAGE) is a technique widely used in biochemistry, forensic chemistry, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility ...

  4. Sodium dodecyl sulfate - Wikipedia

    en.wikipedia.org/wiki/Sodium_dodecyl_sulfate

    For instance, SDS is a component, along with other chain-length amphiphiles, when produced from coconut oil, and is known as sodium coco sulfate (SCS). [26] SDS is available commercially in powder, pellet, and other forms (each differing in rates of dissolution), as well as in aqueous solutions of varying concentrations. [citation needed]

  5. Gel electrophoresis of proteins - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis_of...

    Proteins separated by SDS-PAGE, Coomassie brilliant blue staining. Protein electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium, namely agarose or polyacrylamide.

  6. Two-dimensional gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Two-dimensional_gel...

    The analysis of this sub organelle organisation of the cell requires techniques conserving the native state of the protein complexes. Separate just by mass is commonly achieved using SDS-PAGE. SDS denatures the proteins, breaks apart most complexes, and approximately equalizes the mass-to-charge ratios. SDS must be done as the second ...

  7. Difference gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Difference_gel_electrophoresis

    The three samples are mixed and loaded onto IEF (isoelectric focusing chromatography) for first dimension and the strip is transferred to a SDS PAGE.After the gel electrophoresis, the gel is scanned with the excitation wavelength of each dye one after the other, so each sample can be seen separately (if we scan the gel at the excitation wavelength of the Cy3 dye, we will see in the gel only ...

  8. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different molecules by differences in their isoelectric point (pI). [ 1 ] [ 2 ] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a function of the ...

  9. Eastern blot - Wikipedia

    en.wikipedia.org/wiki/Eastern_blot

    The eastern blot, or eastern blotting, is a biochemical technique used to analyze protein post-translational modifications including the addition of lipids, phosphates, and glycoconjugates. It is most often used to detect carbohydrate epitopes. Thus, eastern blot can be considered an extension of the biochemical technique of western blot.