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Protein Phosphatase 1G 546 a.a. Human Recombinant ( PPM1G Human, 546 a.a. )

DescriptionPPM1G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 566 amino acids (1-546) and having a molecular mass of 61.4 kDa. The PPM1G is fused to a 20 amino acid His-Tag at N-terminus and purified

$193.00

Data sheet

Formulation The PPM1G solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl, 0.1mM PMSF and 20% glycerol.
Purity Greater than 85% as determined by SDS-PAGE.
Description PPM1G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 566 amino acids (1-546) and having a molecular mass of 61.4 kDa. The PPM1G is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Protein Background PPM1G is part of the PP2C family of Ser/Thr protein phosphatases which are known to be negative regulators of cell stress response pathways. PPM1G is accountable for the dephosphorylation of Pre-mRNA splicing factors, an important factor for the formation of functional spliceosome. PPM1G regulates cell cycle progression. PPM1G mediates histone dephosphorylation/exchange in response to DNA damage or checkpoint recovery in higher eukaryotes. The degradation of p21/WAF1 induced by PPM1G is mediated in a proteasome-dependent manner. Protein phosphatase 1G regulates assembly and function of the beta-catenin degradation complex.
Expression host E.coli.
Synonyms Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phosphatase 1C, PPM1G, PPM1C.
Reagent Appearance Sterile Filtered colorless solution.
Stability Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino acid sequence MGSSHHHHHH SSGLVPRGSH MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGPPH SKSGGGTGEE PGSQGLNGEA GPEDSTRETP SQENGPTAKA YTGFSSNSER GTEAGQVGEP GIPTGEAGPS CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE AEEDDEEEEE EMMVPGMEGK EEPGSDSGTT AVVALIRGKQ LIVANAGDSR CVVSEAGKAL DMSYDHKPED EVELARIKNA GGKVTMDGRV NGGLNLSRAI GDHFYKRNKN LPPEEQMISA LPDIKVLTLT DDHEFMVIAC DGIWNVMSSQ EVVDFIQSKI SQRDENGELR LLSSIVEELL DQCLAPDTSG DGTGCDNMTC IIICFKPRNT AELQPESGKR KLEEVLSTEG AEENGNSDKK KKAKRD
Biological Activity Specific activity: >3,000 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme hydrolyzing 1 nmole of p-nitrophenyl phosphate (pNPP) per minute at 25C, pH7.5 using 10mM of substrate.

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