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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 method for separation and ... 1975 – 2-dimensional gels (O’Farrell); isoelectric focusing, then SDS gel electrophoresis;

  5. 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.

  6. Two-dimensional gel electrophoresis - Wikipedia

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

    Two-dimensional gel electrophoresis, abbreviated as 2-DE or 2-D electrophoresis, is a form of gel electrophoresis commonly used to analyze proteins. Mixtures of proteins are separated by two properties in two dimensions on 2D gels. 2-DE was first independently introduced by O'Farrell [ 1 ] and Klose [ 2 ] in 1975.

  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.