MYPT1 (phospho-T853) polyclonal antibody

Myosin phosphatase target subunit 1 (MYPT1), also called Myosin-binding subunit of Myosin phosphatase, is one of the subunits and an integral component of the Myosin phosphatase. Myosin phosphatase regulates the interaction of Actin and Myosin downstream of the guanosine triphosphatase Rho, which inhibits Myosin phosphatase through the action of Rho-kinase. MYPT1 promotor contains one Sp1 transcription factor binding site, suggesting that MYPT1 is a housekeeping gene. Myotonic dystrophy protein kinase phosphorylates MYPT1 at Tyrosine 654 to regulate Myosin II phosphorylation. Inhibition of Myosin light chain phosphatase results in Ca2+ sensitization of smooth muscle contraction. This inhibition is modulated through phosphorylation of MYPT1 by a ZIP-like kinase, which associates with MYPTI and phosphoryl-ates the inhibitory site in smooth muscle. The phosphorylation of MYPT1 by protein kinase C results in altered dephosphoryation of Myosin by attenuating the binding of protein phosphatase 1 catalytic subunit (PP1c) and the phosphorylated Myosin light chain to MYPT1. PP1c interacts with at least four binding sties on the amino-terminus of MYPT1.

Protein phosphatase 1 regulatory subunit 12A; Myosin phosphatase-targeting subunit 1; Myosin phosphatase target subunit 1; Protein phosphatase myosin-binding subunit; PPP1R12A

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of p-MYPT1 (T853) pAb at 1:500 dilution Lane1:Hela whole cell lysate (40ug) Lane2:MCF-7 whole cell lysate (40ug) Lane3:HEK293T whole cell lysate (40ug)