CdGAP Antibody - #AF7024
| Product: | CdGAP Antibody |
| Catalog: | AF7024 |
| Description: | Rabbit polyclonal antibody to CdGAP |
| Application: | ELISA(peptide) |
| Reactivity: | Human, Mouse, Rat, Monkey |
| Mol.Wt.: | 250 kDa(Observed); 157kD(Calculated). |
| Uniprot: | Q2M1Z3 |
| RRID: | AB_2843448 |
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Product Info
Source:
Rabbit
Reactivity:
Human, Mouse, Rat, Monkey
Clonality:
Polyclonal
Specificity:
CdGAP Antibody detects endogenous levels of total CdGAP.
RRID:
AB_2843448
Cite Format: Affinity Biosciences Cat# AF7024, RRID:AB_2843448.
Cite Format: Affinity Biosciences Cat# AF7024, RRID:AB_2843448.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:
Fold/Unfold
ARHGAP31; Cdc42 GTPase-activating protein; RHG31_HUMAN; Rho GTPase-activating protein 31;
Immunogens
Immunogen:
A synthesized peptide derived from human CdGAP, corresponding to a region within the internal amino acids.
Uniprot:
Description:
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 carboxyterminal
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).
Sequence:
- Q2M1Z3 RHG31_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGVTSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHCPEEGQLARIQNVIQELPPSHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKEIEATGCNGDAAFLAVRVQQVVIEFILNHVDQIFNNGAPGSLENDENRPIMKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPMGTLFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKETKGNFNRTVTTGGFFIPATKMHSTGTGSSCDLTKQEGEWGQEGMPPGAEGGFDVSSDRSHLQGAQARPPPEQLKVFRPVEDPESEQTAPKMLGMFYTSNDSPSKSVFTSSLFQMEPSPRNQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFHGSESGGWPEEEKPLGAETSAASVPKKAGLEDAKAVPEAPGTVECSKGLSQEPGAHLEEKKTPESSLSSQHLNELEKRPNPEKVVEEGREAGEMESSTLQESPRARAEAVLLHEMDEDDLANALIWPEIQQELKIIESEEELSSLPPPALKTSPIQPILESSLGPFIPSEPPGSLPCGSFPAPVSTPLEVWTRDPANQSTQGASTAASREKPEPEQGLHPDLASLAPLEIVPFEKASPQATVEVGGPGNLSPPLPPAPPPPTPLEESTPVLLSKGGPEREDSSRKLRTDLYIDQLKSQDSPEISSLCQGEEATPRHSDKQNSKNAASEGKGCGFPSPTREVEIVSQEEEDVTHSVQEPSDCDEDDTVTDIAQHGLEMVEPWEEPQWVTSPLHSPTLKDAHKAQVQGLQGHQLEKRLSHRPSLRQSHSLDSKPTVKSQWTLEVPSSSSCANLETERNSDPLQPQAPRREITGWDEKALRSFREFSGLKGAEAPPNQKGPSGVQPNPAETSPISLAEGKELGTHLGHSSPQIRQGGVPGPESSKESSPSVQDSTSPGEHPAKLQLKSTECGPPKGKNRPSSLNLDPAIPIADLFWFENVASFSSPGMQVSEPGDPKVTWMTSSYCKADPWRVYSQDPQDLDIVAHALTGRRNSAPVSVSAVRTSFMVKMCQARAVPVIPPKIQYTQIPQPLPSQSSGENGVQPLERSQEGPSSTSGTTQKPAKDDSPSSLESSKEEKPKQDPGAIKSSPVDATAPCMCEGPTLSPEPGSSNLLSTQDAVVQCRKRMSETEPSGDNLLSSKLERPSGGSKPFHRSRPGRPQSLILFSPPFPIMDHLPPSSTVTDSKVLLSPIRSPTQTVSPGLLCGELAENTWVTPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE
Research Backgrounds
Function:
Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration.
PTMs:
Phosphorylation on Thr-789 reduces GAP activity.
Subcellular Location:
Cell projection>Lamellipodium. Cell junction>Focal adhesion.
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