bs-70645R

DATASHEET

Host: Rabbit

Target Protein: RhoA (Ser-188)

Specificity: The antibody detects a RhoA GST fusion protein when phosphorylated with PKA, but does not detect the unphosphorylated recombinant protein. This peptide sequence is highly conserved in rat, mouse, and chicken RhoA, but is not found in RhoB or RhoC proteins.

Modification Site: Ser-188

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P06749

Source: Phospho-RhoA (Ser-188) synthetic peptide (coupled to KLH) corresponding to amino acid residues around serine 188 of human RhoA.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Background:

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.