R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
GPNMB (E7U1Z) Rabbit mAb #90205
Filter:
- WB
- IF
- F
Supporting Data
REACTIVITY | M |
SENSITIVITY | Endogenous |
MW (kDa) | 90, 100 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- M-Mouse
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunofluorescence (Frozen) | 1:400 |
Immunofluorescence (Immunocytochemistry) | 1:50 - 1:200 |
Flow Cytometry (Fixed/Permeabilized) | 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) Rabbit mAb recognizes endogenous levels of total mouse GPNMB protein. This antibody does not cross-react with human GPNMB protein.
Species Reactivity:
Mouse
Source / Purification
Monoclonal antibody 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).
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).
- Tomihari, M. et al. (2009) Exp Dermatol 18, 586-95.
- Sheng, M.H. et al. (2012) PLoS One 7, e35280.
- Shikano, S. et al. (2001) J Biol Chem 276, 8125-34.
- Li, B. et al. (2010) FASEB J 24, 4767-81.
- Patel-Chamberlin, M. et al. (2011) Kidney Int 79, 1138-48.
- Bandari, P.S. et al. (2003) Regul Pept 111, 169-78.
- Maric, G. et al. (2013) Onco Targets Ther 6, 839-52.
- Ripoll, V.M. et al. (2007) J Immunol 178, 6557-66.
- Tse, K.F. et al. (2006) Clin Cancer Res 12, 1373-82.
- Rose, A.A. et al. (2010) Clin Cancer Res 16, 2147-56.
- Keir, C.H. and Vahdat, L.T. (2012) Expert Opin Biol Ther 12, 259-63.
- Furochi, H. et al. (2007) FEBS Lett 581, 5743-50.
- Rose, A.A. et al. (2010) PLoS One 5, e12093.
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