Product Pathways - Cytoskeletal Signaling
M-RIP Antibody #11949
|W||H M (R) (Mk) (B) (Dg)||Endogenous||130-140||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey B=Bovine Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
M-RIP Antibody recognizes endogenous levels of total M-RIP protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro62 of human M-RIP protein. Antibodies are purified by protein A and peptide affinity chromatography.
Myosin phosphatase-rho interacting protein (M-RIP), also known as p116RIP, RIP3, and MPRIP, localizes to actin-myosin filaments regulating cytoskeletal dynamics (1-3). M-RIP contains amino-terminal pleckstrin homology domains, carboxyl-terminal coiled-coil domains, and was originally identified to associate with the myosin phosphatase complex. M-RIP binds to MBS/MYRT, the myosin binding subunit of myosin phosphatase, as well as RhoA (1-3). Phosphorylation of MYRT by Rho-associated kinase (ROCK) inhibits myosin phosphatase activity, resulting in increased levels of phosphorylation on myosin light chain, and enhanced contractactility (4,5). M-RIP may function as a scaffolding protein for the complex between the myosin phosphatase complex, Rho/ROCK, and actin (2,6). Silencing of M-RIP results in disassembly of the complex, increased phosphorylation of myosin light chain, and changes to cytoskeletal dynamics (7,8).
- Surks, H.K. et al. (2003) J Biol Chem 278, 51484-93.
- Mulder, J. et al. (2004) Mol Biol Cell 15, 5516-27.
- Gebbink, M.F. et al. (1997) J Cell Biol 137, 1603-13.
- Kimura, K. et al. (1996) Science 273, 245-8.
- Birukova, A.A. et al. (2004) J Cell Physiol 201, 55-70.
- Riddick, N. et al. (2008) J Cell Biochem 103, 1158-70.
- Surks, H.K. et al. (2005) J Biol Chem 280, 42543-51.
- Koga, Y. and Ikebe, M. (2005) J Biol Chem 280, 4983-91.
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