Anti-Serine/Threonine Protein Phosphatase 1β antibody produced in rabbit

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. PP1β is expressed in brain and muscle and microtubules in Drosophila.
Anti-Serine/threonine protein phosphatase 1β specifically recognizes PP1β isoforms from human, mouse, rat and bovine.

synthetic peptide (PRTANPPKKR) corresponding to the C-terminus of the protein phosphatase 1β catalytic subunit (amino acid residues 318-327).

Solution in phosphate buffered saline, pH 7.5, with 0.08% sodium azide.