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文献和实验Purification and Proteomic Analysis of a Nuclear-Insoluble Protein Fraction
, with more than 70% recovery. The LC-fractionated proteins are further separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE). Protein bands are excised, in-gel digested with trypsin, and then analyzed
Combined 3C-ChIP-Cloning (6C) Assay: A Tool to Unravel Protein-Mediated Genome Architecture
of the partners. View larger version (17K): [in this window] [in a new window] Figure 1. Summary of the Combined 3C-ChIP-Cloning (6C) method. For a review of other recent
OUTLINE Ammonium sulphate precipitation is used to purify a protein (in this case an immunoglobulin) from a big volume of liquid phase. PROTOCOL Slowly (!!!) add the solution of ammonium sulphate (40-50% final, v/v
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