PPP1R12A Antibody | 13-210

PPP1R12A Antibody | 13-210 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: N/A

Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 1-200 of human PPP1R12A (NP_002471.1) .

Research Area: Cell Cycle, Signal Transduction

Tested Application: WB, IP

Application: WB: 1:500 - 1:2000
IP: 1:50 - 1:100

Specificiy: N/A

Positive Control 1: U-87MG

Positive Control 2: LO2

Positive Control 3: Jurkat

Positive Control 4: HeLa

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: Observed: 140kDa

Validation: N/A

Isoform: N/A

Purification: Affinity purification

Clonality: Polyclonal

Clone: N/A

Isotype: IgG

Conjugate: Unconjugated

Physical State: Liquid

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Concentration: N/A

Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.

Alternate Name: M13MBS, MYPT1, protein phosphatase 1 regulatory subunit 12A, myosin binding subunit, myosin phosphatase, target subunit 1, myosin phosphatase-targeting subunit 1, protein phosphatase 1, regulatory (inhibitor) subunit 12A, protein phosphatase myosin-binding subunit

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: 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.