Render Target: STATIC
Render Timestamp: 2024-11-21T12:48:14.507Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-04-05 20:48:44.088
Product last modified at: 2024-06-27T13:37:05.817Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

GADS Antibody #48287

Filter:
  • WB

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 40
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    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, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    GADS Antibody recognizes endogenous levels of total GADS protein.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly172 of human GADS protein. Antibodies are purified by peptide affinity chromatography.

    Background

    GRB2-related adaptor downstream of Shc (GADS) belongs to the GRB2 family of adaptor proteins. It is a hematopoietic cell-specific signaling adaptor protein that harbors amino- and carboxy-terminal SH3 domains, a central SH2 domain, and a unique linker region that is rich in proline and glutamine residues (1). The presence of SH2 and SH3 domains within GADS strongly suggest that it functions in signal transduction cascades by facilitating protein-protein interactions. In the context of T cells, research studies have demonstrated that GADS interacts with LAT and SLP-76 signaling complexes to facilitate NFAT activation downstream of TCR engagement (2-4). Given its role as a fundamental mediator of TCR signaling, GADS is subject to multiple modes of negative regulation to limit TCR signal strength. For example, research studies have demonstrated that HPK1 directly phosphorylates GADS at Thr262 within its linker region, a modification that promotes 14-3-3 binding and dissociation of signaling complexes nucleated by LAT, SLP-76, and GADS (5). The linker region of GADS is also subject to caspase-mediated cleavage, which separates its SH2 and SH3 domains and thus impairs the ability of GADS to bridge LAT and SLP-76 signaling complexes for transduction of faithful TCR signals (6,7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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