Western blot analysis of extracts from 293 cells, untreated or treated with the ROCK inhibitor Y27632 (2 minutes at 10µM) using MYPT1 (pT696) Polyclonal Antibody or a total MYPT1 antibody. MYPT1 (pT696) Polyclonal Antibody was pre-incubated as indicated with phospho-MYPT1 (Thr696) peptide or nonphospho-MYPT1 (Thr696) peptide.
|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic phosphopeptide corresponding to residues surroundiing Thr696 of human MYPT1|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 50% glycerol, 100µg/ml BSA|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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 this gene.
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