Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described.
Protein phosphatase 2C(PP2C?) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.
Protein Phosphatase 1A Alpha Isoform Human Recombinant produced is a single, non-glycosylated polypeptide chain containing 382 amino acids and having a molecular mass of 46.6KDa (containing His tag, T7 gene 10 leader, XpressTM Epitope). The protein coding region of PP2C? (amino acids 1-382) was cloned into an E. coli expression vector(BamHI/Hind? site). PPM1A was overexpressed in E. coli as a soluble His-tag fusion protein, and it was purified by conventional column chromatographic techniques.
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