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Render Timestamp: 2024-10-11T10:50:55.045Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-08-01 15:30:52.608
Product last modified at: 2024-05-30T07:06:56.506Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

ADAM10 Antibody #14194

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  • WB
  • IP
This product is discontinued

Inquiry Info. # 14194

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    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 68, 90
    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

    ADAM10 Antibody recognizes endogenous levels of total ADAM10 protein, including the active, mature 68 kDa protein and the 90 kDa precursor chain. The antibody also recognizes a 35 kDa protein of unknown origin.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human ADAM10 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Members of the ADAM (a disintegrin and a metalloprotease) family of multidomain membrane proteins influence cell signaling and adhesion by shedding cell surface proteins, such as cytokines and growth factors. This process influences cell-extracellular matrix (ECM) adhesion and ECM remodeling. Conserved domains found in most ADAM family proteins include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a carboxy-terminal cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2).
    The ADAM metallopeptidase domain 10 (ADAM10) is a plasma membrane proteinase that cleaves membrane-bound proteins targeted for regulated intramembrane proteolysis (RIP). The ADAM10 prodomain acts as a chaperone that stabilizes mature ADAM protein folding, and prevents target-protein shedding through inhibition of ADAM10 proteinase activity (3,4). Mature ADAM10 is the major α-secretase responsible for cleavage of Notch, APP, cadherins, and prion protein (5-7). The ADAM10 protein cleaves receptor tyrosine kinases and their associated ligands and displays a wide range of regulatory functions across related signaling pathways (8). Research studies using knockout mice demonstrate that loss of ADAM10 results in defects in cortex formation, lymphocyte development, and cardiovascular development (9-11). Increased ADAM10 protein expression correlates with progression of many types of cancer (i.e. gastric cancer, hepatocellular carcinoma, and brain glioma), due to increased cancer cell migration, metastasis, and invasion (12-14). Mutations in the corresponding ADAM10 gene result in a rare, autosomal dominant pigmentation disorder known as reticulate acropigmentation of Kitamura (15).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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