PPM1G, 50 µg

The Ser/Thr-specific phosphatases can be divided into two major families: the PPP family, which includes PP1, PP2A, PP2B/calcineurin and the PPM family composed of PP2C. PPM1G/PP2Cγ is a member of the PP2C family, sharing only 34% sequence identity to the α- and β-isoform of PP2C. The PPM group has a strict requirement for divalent metal ions (Mg2+, Mn2+) and is insensitive to known PPP inhibitors. PPM1G/PP2Cγ consists of an additional region of approximately 200 residues not found in other PP2Cs. This domain of acidic amino acids is probably important for cellular targeting and plays a crucial role in determining substrate specificity. PPM1G/PP2Cγ is involved in mRNA splicing processes cause it is associated with the spliceosome and required during the early stages of spliceosome assembly for efficient formation of the A complex. 

Protein Informations: PPM1G human, recombinant fused with His-tag at N-terminus is a single, non-glycosylated, polypeptide chain containing 250 amino acids (aa 370-547) and having a molecular mass of 27 kDa. The PRMT1 is purified by proprietary chromatographic techniques. Protein concentration: 1.0 mg/ml, Purity: > 95% by SDS PAGE

Ordering information: shipped on dry ice

Product specific literature:

Lu G, Wang Y. (2008) "Functional diversity of mammalian type 2C protein phosphatase isoforms: new tales from an old family." Clin Exp Pharmacol Physiol. 35(2):107-12.

Murray MV, Kobayashi R, Krainer AR. (1999) "The type 2C Ser/Thr phosphatase PP2Cgamma is a pre-mRNA splicing factor." Genes Dev. 1; 13 (1):87-97.

Jackson MD, Denu JM. (2001) "Molecular reactions of protein phosphatases--insights from structure and chemistry." Chem Rev. 101(8):2313-40.

Travis SM, Welsh MJ. (1997) "PP2C gamma: a human protein phosphatase with a unique acidic domain." FEBS Lett. 4;412 (3):415-9.

Product Citations:

Vogel S, Grabski E, Buschjäger D, Klawonn F, Döring M, Wang J, Fletcher E, Bechmann I, Witte T, Durisin M, Schraven B Mangsbo SM, Schönfeld K, Czeloth N, Kalinke U. (2015) "Antibody induced CD4 down-modulation of T cells is site-specifically mediated by CD64(+) cells." Sci Rep. 16;5:18308