mouse monoclonal IgG2b; PP1 Antibody (E-9) is an IgG2b κ mouse monoclonal PP1 antibody (also designated PPP1CA antibody, PPP1A antibody, or serine/threonine-protein phosphatase PP1-alpha catalytic subunit antibody) that detects the PP1 protein of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA. PP1 Antibody (E-9) is available as both the non-conjugated anti-PP1 antibody form, as well as multiple conjugated forms of anti-PP1 antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP1 family is comprised of subfamily members PP1α, PP1β and PP1γ, which are MgATP-dependent enzymes. PP1 inactivity is maintained through its association with the inhibitory protein NIPP-1 (nuclear inhibitor of PP1). Phosphorylation of NIPP-1 by cAMP-PK or casein kinase II results in the release of active PP1.