Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP. RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for PPP1R12A
Clonality
Polyclonal
Formulation
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen
Host
Rabbit
Immunogen
Synthesized peptide derived from human MYPT1 around the non-phosphorylation site of T696
Isotype
Rabbit IgG
Reactivity
Human, Mouse, Rat, Monkey
Gene Id
4659
Concentration
1 mg/ml
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen
Storage Buffer
PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide