Render Target: SSR
Render Timestamp: 2025-03-16T06:30:01.051Z
Commit: a619ae74f66dae0f27639e88da12bcf600e46428
XML generation date: 2025-03-07 13:09:20.560
Product last modified at: 2025-01-01T09:04:31.620Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

EphA2 Antibody #3974

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Inquiry Info. # 3974

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    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 135
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    EphA2 Antibody detects endogenous levels of total EphA2 protein. It does not cross-react with other related proteins.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr930 of human EphA2. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).
    EphA2 is overexpressed in various tumor cells and it has been suggested that EphA2 may promote malignancy. However, several studies demonstrate that EphA2 plays an important role in tumor suppression (8). The role of EphA2 in tumor development may depend upon regulation of its tyrosine kinase activity.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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