Render Target: STATIC
Render Timestamp: 2024-10-31T09:51:58.413Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-08-01 15:28:13.036
Product last modified at: 2024-10-21T13:15:09.483Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

GPNMB Antibody #56898

Filter:
  • WB

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 90-100
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • 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

    GPNMB Antibody recognizes endogenous levels of total mouse GPNMB protein. This antibody does not cross-react with human GPNMB protein.

    Species Reactivity:

    Mouse

    Source / Purification

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

    Background

    Glycoprotein non-metastatic gene B (GPNMB) is a type I transmembrane glycoprotein overexpressed in many types of cancer. The GPNMB glycoprotein is involved in many physiological processes, including mediating transport of late melanosomes to keratinocytes (1), regulating osteoblast and osteoclast differentiation and function (2), stimulating dendritic cell maturation, promoting adhesion of dendritic cells to endothelial cells (3), enhancing autophagosome fusion to lysosomes in tissue repair, and regulating degradation of cellular debris (4,5).

    While typical GPNMB expression is seen in tissues including skin, heart, kidney, lung, liver, and skeletal muscle (3,6), research studies show elevated GPNMB expression often contributes to the metastatic phenotype in numerous cancers (reviewed in 7). GPNMB is typically localized to intracellular compartments in normal cells (1,8), but investigators found it primarily on the cell surface of tumor cells (9,10). Differential localization and expression, and the role of GPNMB as a tumor promoter in many cancer types make this protein a viable therapeutic target (11).

    The GPNMB ectodomain can be cleaved by matrix metalloproteinases and shed from the cell surface (12). Research studies identify the sheddase ADAM10 as one peptidase responsible for cleavage of the GPNMB ectodomain at the surface of breast cancer cells. Shedded GPNMB ectodomains may promote angiogenesis by inducing endothelial cell migration (13).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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