Rho (A, B, & C) proteins are members of the Ras superfamily of GTPases. These proteins regulate a variety of cellular functions, including cell cycle progression, cytoskeletal rearrangement, and gene expression. Rho cycles between the active GTP-bound form and an inactive GDP-bound form. Interconversion between these forms is controlled by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). The Rho proteins RhoA, RhoB, and RhoC are highly homologous and contain the consensus amino acid sequences necessary for GDP/GTP-binding and GTPase activity. Post-translational regulation of Rho activity has been shown specifically for RhoA. This Rho protein is phosphorylated in vitro on serine 188 by cAMP- and cGMP-dependent kinases (PKA and PKG). Ser-188 phosphorylation enhances RhoGDI binding and inhibits RhoA-mediated stress fiber formation. Thus, Ser-188 is an important site for negative regulation of RhoA activity.
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*For more information, see UniProt Accession P06749
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Giralt, A. et al. (2016) Glia. 64(4):620 (WB: mouse astrocyte)
Utsumi, T. et al. (2014)J Urol. 192(2):567 (WB: 786-O cells)
Selimovic, D. et al. (2013) Apoptosis. 18(8):980. (WB: human melanoma cells)
Harma, V. et al. (2012) Oncogene. 31:2075. (WB: human PC-3 cells)
Xu, J. et al. (2011) Int J Cancer. Online Mar 8. (WB: rat lymphatic ECs)
This kit contains: