Product Pathways - Cytoskeletal Signaling
p190-B RhoGAP Antibody #2562
|W||H M R Mk B||Endogenous||190||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
p190-B RhoGAP Antibody detects endogneous levels of total RhoGAP protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to a region surrounding Lys296 of human p190-B RhoGAP. Antibodies are purified by protein A and peptide affinity chromatography.
Rho family GTPases are key regulators of diverse processes such as cytoskeletal organization, cell growth and differentiation, transcriptional regulation, and cell adhesion/motility. The activities of these proteins are controlled primarily through guanine nucleotide exchange factors (GEFs) that facilitate the exchange of GDP for GTP, promoting the active (GTP-bound) state, and GTPase activating proteins (GAPs) that promote GTP hydrolysis and the inactive (GDP-bound) state (1,2).The p190 RhoGAP proteins are widely expressed Rho family GAPs. p190-A has been characterized as a tumor suppressor, and research studies have shown that loss or rearrangement of the chromosomal region containing the gene for p190-A is linked to tumor development (3,4). p190-A binds the mitogen-inducible transcription factor TFII-I, sequestering it in the cytoplasm and inhibiting its activity. Phosphorylation of p190-A at Tyr308 reduces its affinity for TFII-I, relieving the inhibition (5). p190-A can also inhibit growth factor-induced gliomas in mice (6) and affect cleavage furrow formation and cytokinesis in cultured cells (7).Mice lacking p190-B RhoGAP show excessive Rho activation and a reduction in activation of the transcription factor CREB (8). Cells deficient in p190-B display defective adipogenesis (9). There is increasing evidence that p190 undergoes tyrosine phosphorylation, which activates its GAP domain (9-11). Levels of tyrosine phosphorylation are enhanced by Src overexpression (10,11). IGF-I treatment downregulates Rho through phosphorylation and activation of p190-B RhoGAP, thereby enhancing IGF signaling implicated in adipogenesis (9).
- Peck, J. et al. (2002) FEBS Lett. 528, 27-34.
- Moon, S.Y. and Zheng, Y. (2003) Trends Cell Biol. 13, 13-22.
- Wang, Z. et al. (1996) Cell Growth Differ 7, 123-33.
- Tikoo, A. et al. (2000) Gene 257, 23-31.
- Jiang, W. et al. (2005) Mol Cell 17, 23-35.
- Wolf, R.M. et al. (2003) Genes Dev 17, 476-87.
- Su, L. et al. (2003) J Cell Biol 163, 571-82.
- Sordella, R. et al. (2002) Dev Cell 2, 553-65.
- Sordella, R. et al. (2003) Cell 113, 147-58.
- Chang, J.H. et al. (1995) J Cell Biol 130, 355-68.
- Roof, R.W. et al. (1998) Mol Cell Biol 18, 7052-63.
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For Research Use Only. Not For Use In Diagnostic Procedures.