Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. Protein phosphatases, like kinases, are a class of enzymes that regulate protein phosphorylation. The serine/threonine phosphatases have been classified into four groups which include PP1, PP2A, PP2B (also termed calcineurin) and PP2C on the basis of differences in their biochemical properties. PP1 catalyzes a wide range of protein dephosphorylation reactions in a tightly regulated manner and is expressed abundantly in the brain. PP1 has broad functions covering glycogen metabolism, protein synthesis, cell cycle and growth and muscle contractility. PP1 forms exclusive complexes with >50 regulatory subunits that allows for restricted subcellular location and thereby distinct cellular functions. There are 3 isoforms of PP1 (α, β and γ1) with 90% homology. PP1α is expressed in brain and muscle. Anti-Serine/threonine protein phosphatase 1α specifically recognizes PP1α isoform and recognizes an epitope within its catalytic subunit (36 kDa) in human, mouse, rat and bovine.
Specificity
By immunoblotting, the antibody specifically reacts with protein phosphatase 1α and recognizes an epitope within its catalytic subunit. The sequence is identical in rabbit PP1α.
Immunogen
synthetic peptide corresponding to amino acids 316-328 of the human protein phosphatase 1α (catalytic subunit) on a synthetic MAP carrier.
Application
A minimum dilution of 1:2000 of Anti-PP1α is used for detection by immunoblotting in whole cell extracts of A431, human epidermoid carcinoma cell line. The antibody is also suitable for protein microarray.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The microcystin (MC) producing P. rubescens occurs in pre-alpine lakes and may impact fishery success, bathing, and raw water quality. P. rubescens extracts, characterized via LC-MS, contained the two MC-RR variants [Asp3]MC-RR and [Asp3,Dhb7]MC-RR. The protein-phosphatase-inhibition assay (cPPIA with phosphatases
The Journal of comparative neurology, 413(3), 373-384 (1999-09-29)
Protein phosphatase 1 (PP1) is a gene family with a number of important functions in brain. Association with a wide variety of regulatory/targeting subunits is thought to be instrumental in directing the phosphatase to specific subcellular locations and substrates. By
Journal of cell science, 115(Pt 2), 241-256 (2002-02-13)
Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits. Most of these target
Trends in biochemical sciences, 35(8), 450-458 (2010-04-20)
Protein Ser/Thr phosphatase-1 (PP1) catalyzes the majority of eukaryotic protein dephosphorylation reactions in a highly regulated and selective manner. Recent studies have identified an unusually diversified PP1 interactome with the properties of a regulatory toolkit. PP1-interacting proteins (PIPs) function as
Serine/threonine protein phosphatases.
S Wera et al.
The Biochemical journal, 311 ( Pt 1), 17-29 (1995-10-01)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.