|Products||PPase-2A from Promega|
|Description||Protein Phosphatase-2A (PPase-2A) is a serine/threonine phosphatase isolated from human red blood cells. It is isolated as the heterodimer of 60kDa (A) and 36kDa (C) subunits. It has the ability to dephosphorylate the a-subunit of phosphorylase kinase. With its 3638kDa catalytic subunit, PPase-2A has broad substrate specificity and may play a regulatory role in DNA replication, transcription, protein synthesis, mitosis and glycogen metabolism. PPase-2A is stimulated in vitro by basic proteins such as protamine, histones and polylysine. The enzyme is inhibited by several environmental toxins and tumor promoters such as okadaic acid and microcystin-LR. The chemically synthesized phosphopeptide, RRA(pT)VA (available in the Ser/Thr Phosphatase Assay System, Cat.# V2460), is an excellent substrate for PPase-2A.|
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