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Protein Phosphatase 1, Catalytic Subunit Alpha Human Recombinant ( PPP1CA Human )

DescriptionPPP1CA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-330 a.a) and having a molecular mass of 39.7kDa.PPP1CA is fused to a 20 amino acid His-tag at N-terminus &

$193.00

Data sheet

Formulation PPP1CA protein solution (0.2mg/ml) containing 50mM Tris-HCl (pH8.5),0.2M NaCl, 1mM DTT, 0.1mM PMSF, 1mM MnCl2 and 50% glycerol.
Purity Greater than 80.0% as determined by SDS-PAGE.
Description PPP1CA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-330 a.a) and having a molecular mass of 39.7kDa.PPP1CA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Protein Background Serine/Threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA) is crucial for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. The PPP1CA protein may have a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.
Expression host Escherichia Coli.
Synonyms Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PP-1A, PPP1CA, PPP1A, PP1alpha.
Reagent Appearance Sterile filtered yellowish 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 MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK.
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 37C, pH7.5 using 10mM of substrate.

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