Render Target: STATIC
Render Timestamp: 2024-11-01T09:53:34.951Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-09-30 01:54:00.354
Product last modified at: 2024-09-30T08:02:33.365Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

CdGAP (D6J9G) Rabbit mAb #14087

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 250
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    CdGAP (D6J9G) Rabbit mAb recognizes endogenous levels of total CdGAP protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser520 of human CdGAP protein.

    Background

    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.
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