Render Target: STATIC
Render Timestamp: 2024-12-20T11:54:35.143Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-12-11 20:05:14.309
Product last modified at: 2024-12-12T17:15:17.803Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-DDR1 (Tyr792) Antibody #11994

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 125
    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 1:50

    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

    Phospho-DDR1 (Tyr792) Antibody recognizes endogenous levels of DDR1 protein only when phosphorylated at Tyr792. This antibody may cross-reacts with other tyrosine-phosphorylated RTKs.

    Species Reactivity:

    Human

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr792 of human DDR1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The discoidin domain receptors (DDRs) are receptor tyrosine kinases with a discoidin homology repeat in their extracellular domains, activated by binding to extracellular matrix collagens. So far, two mammalian DDRs have been identified: DDR1 and DDR2 (1). They are widely expressed in human tissues and may have roles in smooth muscle cell-mediated collagen remodeling (2). Research studies have implicated aberrant expression and signaling of DDRs in human diseases related to increased matrix degradation and remodeling, such as cardiovascular disease, liver fibrosis, and tumor invasion (1).

    Phosphorylation of DDR1 at Tyr792 was identified at Cell Signaling Technology using PTMScan®, our LC-MS/MS platform for phosphorylation site discovery (3). Tyr792 is located in the activation loop of the DDR1 kinase domain.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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