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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. 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.

  4. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Gel electrophoresis is an electrophoresis ... the molecules through the gel, and a positive charge at the other end that pulls the molecules through the gel ...

  5. Polyacrylamide gel electrophoresis - Wikipedia

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

    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. Electrophoretic mobility is a function of the length, conformation, and ...

  6. Western blot - Wikipedia

    en.wikipedia.org/wiki/Western_blot

    SDS-PAGE electrophoresis. The proteins of the sample are separated using gel electrophoresis. Separation of proteins may be by isoelectric point (pI), molecular weight, electric charge, or a combination of these factors. The nature of the separation depends on the treatment of the sample and the nature of the gel.

  7. Protein mass spectrometry - Wikipedia

    en.wikipedia.org/wiki/Protein_mass_spectrometry

    The first-dimension of 2D gel is isoelectric focusing (IEF). In this dimension, the protein is separated by its isoelectric point (pI) and the second-dimension is SDS-polyacrylamide gel electrophoresis (SDS-PAGE). This dimension separates the protein according to its molecular weight. [10] Once this step is completed in-gel digestion occurs.

  8. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    Isoelectric focusing is the first step in two-dimensional gel electrophoresis, in which proteins are first separated by their pI value and then further separated by molecular weight through SDS-PAGE. Isoelectric focusing, on the other hand, is the only step in preparative native PAGE at constant pH. [5]

  9. Molecular-weight size marker - Wikipedia

    en.wikipedia.org/wiki/Molecular-weight_size_marker

    The purpose of gel electrophoresis is to separate proteins by physical or chemical properties, which include charge, molecular size, and pH.< When separating based on size, the ideal method is SDS-PAGE or polyacrylamide gel electrophoresis and molecular-weight size markers are the appropriate standards to use.