Recombinant Human Osteoactivin/GPNMB Fc Chimera Protein, CF Summary
Details of Functionality
Measured by the ability of the immobilized protein to induce pro-MMP-9 secretion by NHLF human normal lung fibroblasts The ED50 for this effect is 2.5-10 µg/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human Osteoactivin/GPNMB protein
Human Osteoactivin (Lys23 - Asn486) Accession #NP_002501
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
78.6 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
115-125 kDa, reducing conditions
Publications
Read Publications using 2550-AC in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Osteoactivin/GPNMB Fc Chimera Protein, CF
DC-HIL
glycoprotein (transmembrane) nmb
glycoprotein NMB
GPNMB
HGFIN
HGFINglycoprotein nmb-like protein
NMBosteoactivin
Osteoactivin
Transmembrane glycoprotein HGFIN
transmembrane glycoprotein NMB
Background
Osteoactivin (also GPNMB and DC-HIL) is a variably glycosylated 75 - 125 kDa member of the NMB/pMEL-17 family of molecules. It is found in multiple subcellular sites, but is most often associated with the endosomal/lysosomal compartment (1, 2, 3). Human Osteoactivin is a 560 amino acid (aa) type I transmembrane protein. Its precursor contains a 21 aa signal sequence, a 465 aa luminal/extracellular domain, a 21 aa transmembrane segment and a 53 aa cytoplasmic tail (4, 5). The luminal region contains an N-terminal heparin-binding motif (aa 23 - 26), multiple glycosylation sites, an RGD motif (aa 64 - 66) and an 88 aa PKD domain (aa 240 - 327). The intracellular tail has an ITAM (Y-x-x-I) and lysosomal targeting (L-L) motif (4, 5). The extracellular/luminal region shares 74% and 77% aa identity with the equivalent regions in mouse and canine, respectively. Multiple isoforms would appear to exist. There is one alternate splice form known that shows a 12 aa insert between aa 339 - 340 (6). An addtional 206 aa isoform shows a mutation at position # 181 that results in a 26 aa substitution for the C-terminal 380 amino acids (7, 8). This has the potential to be soluble and may represent a counterpart to a secreted isoform of rat Osteoactivin (9). Cells known to express Osteoactivin include macrophages/Kupffer cells, fibroblasts, osteoblasts, myeloid dendritic cells, retinal pigment epithelial cells and melanocytes, plus fetal chondrocytes and stratum basale keratinocytes (3, 4, 5, 10, 11, 12). In mice, Osteoactivin is reported to bind to heparan sulfate-proteoglycan, possibly on the surface of endothelial cells and may also interact with integrins (13). It also appears to act as an inflammatory suppressor gene, as its expression downregulates the macrophage inflammatory response by inhibiting IL-6 and IL-12p40 production (3).
Bachner, D. et al. (2002) Gene Exp. Patterns 1:159.
Safadi, F.F. et al. (2002) J. Cell. Biochem. 84:12.
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