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CdGAP Antibody #6954
This product is discontinued
Gallery: CdGAP Antibody #6954
CdGAP Antibody detects endogenous levels of total CdGAP protein. In certain cell lines, CdGAP Antibody recognizes a 125 kDa band of unknown origin.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the central region of human CdGAP protein. Antibodies are purified by protein A and peptide affinity chromatography.
The Rho family of small GTPases, including Rho, Rac, and Cdc42, act as molecular switches that regulate processes such as cell migration, adhesion, proliferation, and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP (1). The serine- and proline-rich GAP protein, Cdc42 GAP (CdGAP), has been shown to be a negative regulator of both Cdc42 and Rac1, but not RhoA (2,3). This protein contains three domains: an amino-terminal GAP domain, a central domain, and a carboxy-terminal proline-rich domain containing five Src homology 3 (SH3)-binding sites. It is suggested that threonine and serine phosphorylation within the proline-rich domain likely alters protein-protein interactions and determines the localization of CdGAP (4). Phosphorylation of CdGAP on threonine 776 by both ERK-1 and GSK-3 has been shown to negatively regulate protein activity, possibly by inducing a conformational change within the protein disrupting its ability to bind SH3 domains (4,5). Upregulation of CdGAP has been shown to increase cell proliferation and it has been suggested that this protein may play a role in TGF-β-induced cell growth, motility, and invasion in some breast cancer cells (6).
For Research Use Only. Not For Use In Diagnostic Procedures. Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.