Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

CdGAP Antibody #6954

Applications Reactivity Sensitivity MW (kDa) Source
W H M Endogenous 250 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

CdGAP Antibody detects endogenous levels of total CdGAP protein. In certain cell lines, CdGAP Antibody recognizes a 125 kDa band of unknown origin.

Source / Purification

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cells lines using CdGAP Antibody.

Background

The Rho family of small GTPases, including Rho, Rac and Cdc42, act as molecular switches, regulating 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 N-terminal GAP domain, a central domain, and a C-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). Phopshorylation 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 it’s 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).

  1. Takai, Y. et al. (2001) Physiol Rev 81, 153-208.
  2. Tcherkezian, J. et al. (2006) Biol Cell 98, 445-56.
  3. Lamarche-Vane, N. and Hall, A. (1998) J Biol Chem 273, 29172-7.
  4. Tcherkezian, J. et al. (2005) Mol Cell Biol 25, 6314-29.
  5. Danek, E.I. et al. (2007) J Biol Chem 282, 3624-31.
  6. He, Y. et al. (2010) Oncogene , .

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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