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GPNMB (E7U1Z) Horse Chimeric mAb #28318

Filter:
  • IF

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Horse chimeric IgG4
    Application Key:
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Description

    This Cell Signaling Technology® antibody retains the antigen-binding Fab regions of the original parent host sequence from which it is engineered. This antibody is expected to exhibit the same species cross-reactivity as GPNMB (E7U1Z) Rabbit mAb #90205.

    Product Usage Information

    Application Dilution
    Immunofluorescence (Frozen) 1:50 - 1:200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    GPNMB (E7U1Z) Horse Chimeric mAb recognizes endogenous levels of total GPNMB protein. This antibody does not cross-react with human GPNMB protein.


    Species Reactivity:

    Mouse

    Source / Purification

    This recombinant chimeric antibody is engineered from GPNMB (E7U1Z) Rabbit mAb #90205 according to animal-free protocols. The chimeric antibody retains its antigen-binding Fab regions from the original rabbit monoclonal antibody but contains a horse-derived Fc domain. When multiplexing, Fc-directed rabbit secondaries are required to detect rabbit-host primary antibodies.

    The parent antibody, GPNMB (E7U1Z) Rabbit mAb #90205, is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of mouse GPNMB protein.

    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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