Render Target: STATIC
Render Timestamp: 2024-11-21T13:53:35.795Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:26:08.828
Product last modified at: 2024-05-30T07:13:48.862Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Girdin Antibody #14200

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 220, 250
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100

    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

    Girdin Antibody recognizes endogenous levels of total girdin protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu1451 of human girdin protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The actin-binding protein girdin (CCDC88A, GIV) is a non-receptor guanine nucleotide exchange factor (GEF) and part of a scaffold that mediates key signaling pathways during cell migration (1). Girdin protein structure includes an amino-terminal Hook domain for microtubule interaction, a coiled-coil dimerization domain, a Gα binding domain, a PI(4)P-binding domain, and a carboxy-terminal receptor-binding domain within a GEF motif (1-5). Akt kinase phosphorylates girdin at Ser1416, which promotes PI(4)P binding, localization of girdin to the membrane leading edge, and regulation of actin organization and cell motility (3). After growth factor receptor activation, girdin binds both G-protein and receptor to form an activation complex at the receptor cytoplasmic tail. The activation complex enhances receptor autophosphorylation and promotes downstream signaling that results in actin organization and cell migration (5). An activated growth factor phosphorylates girdin at its carboxy-terminal Tyr1764 and Tyr1798 residues to form an SH2 docking site for PI3K binding (6). The girdin GEF motif interacts with Gα and leads to release of Gβγ, resulting in further PI3K activation and the completion of signal transduction from receptor to cytoskeleton (7). The cytoskeletal reorganization and cell migration properties of girdin are important in regulating several biological processes, including wound healing, angiogenesis, and cancer progression (8-11).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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