R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
M-RIP (D8G8R) Rabbit mAb #14396
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 130-140 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
M-RIP (D8G8R) Rabbit mAb recognizes endogenous levels of total M-RIP protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro62 of human M-RIP protein.
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 contractility (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.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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