Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

M-RIP Antibody #11949

Applications Reactivity Sensitivity MW (kDa) Source
W H M (R) (Mk) (B) (Dg) Endogenous 130-140 Rabbit

Applications Key:  W=Western Blotting
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.

Protocols

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using M-RIP Antibody.

Background

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).

  1. Surks, H.K. et al. (2003) J Biol Chem 278, 51484-93.
  2. Mulder, J. et al. (2004) Mol Biol Cell 15, 5516-27.
  3. Gebbink, M.F. et al. (1997) J Cell Biol 137, 1603-13.
  4. Kimura, K. et al. (1996) Science 273, 245-8.
  5. Birukova, A.A. et al. (2004) J Cell Physiol 201, 55-70.
  6. Riddick, N. et al. (2008) J Cell Biochem 103, 1158-70.
  7. Surks, H.K. et al. (2005) J Biol Chem 280, 42543-51.
  8. Koga, Y. and Ikebe, M. (2005) J Biol Chem 280, 4983-91.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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