GPNMB Antibody [J15J20] | Primary Antibodies

Application: Reactivity: Human

Lane 1: SK-BR-3

Usage Information

Dilution
WB1:1000 IP1:50 IHC1:250-1:1000

Application
WB, IP, IHC

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
95 kDa, 120 kDa

Datasheet & SDS

Biological Description

Specificity
GPNMB Antibody [J15J20] detects endogenous levels of total GPNMB protein.

Clone
J15J20

Synonym(s)
Transmembrane glycoprotein NMB; Hematopoietic growth factor inducible neurokinin-1 type; GPNMB; HGFIN; NMB

Background
GPNMB, or glycoprotein non-metastatic melanoma protein B, belongs to the type I transmembrane glycoprotein family and serves as a multifaceted regulator of cellular adhesion, migration, and lysosomal dynamics across diverse tissues. It features an N-terminal polycystic kidney disease-like domain, an RGD integrin-binding motif, a cleaved ectodomain, and a short cytoplasmic tail with a hemITAM motif that recruits signaling adaptors. GPNMB localizes primarily to intracellular compartments in normal cells but translocates to the plasma membrane in cancer, where ADAM10-mediated ectodomain shedding releases soluble GPNMB that binds endothelial integrins to trigger VEGF/NRP-1 signaling, FAK activation, and directed migration essential for angiogenesis; full-length GPNMB engages α5β1 integrin via its RGD motif to drive PI3K/AKT/mTOR and ERK/MAPK cascades that upregulate MMP-2/9 for matrix remodeling and ZEB1 for epithelial-mesenchymal transition. GPNMB silencing suppresses proliferation, invasion, and tube formation by downregulating MMP-3 and HIF1α while elevating apoptosis, revealing its central role in tumor-stroma crosstalk where shed ectodomain recruits endothelial support for vascular mimicry in glioma and breast cancer cells. GPNMB governs melanosome transfer to keratinocytes, osteoblast/osteoclast differentiation through RANKL modulation, and dendritic cell maturation via adhesion to VCAM-1, positioning it as a prime target for researchers dissecting lysosomal biogenesis or immune cell trafficking in tissue repair models. Its expression in skin, heart, kidney, and muscle supports homeostasis through autophagy-lysosome flux and debris clearance, with tissue-specific shedding controlled by HB-EGF/EGFR phosphorylation. Dysregulation through overexpression correlates with metastasis in melanoma, glioma, and triple-negative breast cancer, where surface localization predicts poor outcome.

Background

GPNMB, or glycoprotein non-metastatic melanoma protein B, belongs to the type I transmembrane glycoprotein family and serves as a multifaceted regulator of cellular adhesion, migration, and lysosomal dynamics across diverse tissues. It features an N-terminal polycystic kidney disease-like domain, an RGD integrin-binding motif, a cleaved ectodomain, and a short cytoplasmic tail with a hemITAM motif that recruits signaling adaptors. GPNMB localizes primarily to intracellular compartments in normal cells but translocates to the plasma membrane in cancer, where ADAM10-mediated ectodomain shedding releases soluble GPNMB that binds endothelial integrins to trigger VEGF/NRP-1 signaling, FAK activation, and directed migration essential for angiogenesis; full-length GPNMB engages α5β1 integrin via its RGD motif to drive PI3K/AKT/mTOR and ERK/MAPK cascades that upregulate MMP-2/9 for matrix remodeling and ZEB1 for epithelial-mesenchymal transition. GPNMB silencing suppresses proliferation, invasion, and tube formation by downregulating MMP-3 and HIF1α while elevating apoptosis, revealing its central role in tumor-stroma crosstalk where shed ectodomain recruits endothelial support for vascular mimicry in glioma and breast cancer cells. GPNMB governs melanosome transfer to keratinocytes, osteoblast/osteoclast differentiation through RANKL modulation, and dendritic cell maturation via adhesion to VCAM-1, positioning it as a prime target for researchers dissecting lysosomal biogenesis or immune cell trafficking in tissue repair models. Its expression in skin, heart, kidney, and muscle supports homeostasis through autophagy-lysosome flux and debris clearance, with tissue-specific shedding controlled by HB-EGF/EGFR phosphorylation. Dysregulation through overexpression correlates with metastasis in melanoma, glioma, and triple-negative breast cancer, where surface localization predicts poor outcome.

References
https://pubmed.ncbi.nlm.nih.gov/38614127/ https://pubmed.ncbi.nlm.nih.gov/20711474/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%