Recombinant Cyno/Rhesus Osteoactivin/GPNMB Fc Protein, CF

2 μg/lane of Recombinant Cynomolgus/Rhesus Osteoactivin/GPNMB Fc Chimera Protein (Catalog # 11154-AC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 111-122 kDa and 220-245 kDa, respectively.

• Reactivity: Pm-Cm, RM
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Cyno/Rhesus Osteoactivin/GPNMB Fc Protein, CF Summary

• Additional Information: Cynomolgus Monkey/Rhesus Macaque Fc Chimera
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Integrin alpha V beta 3 (Catalog # 3050-AV) is immobilized at 2 µg/mL (100 µL/well), Recombinant Cynomolgus Monkey/Rhesus Macaque Osteoactivin/GPNMB Fc Chimera (Catalog # 11154-AC) binds with an ED₅₀ of 0.750-9.00 µg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived Osteoactivin/GPNMB protein
  

  Cyno/Rhesus Osteoactivin (Lys23-Asn487) Accession # XP_005550047.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: XP_005550047.1
• N-terminal Sequence: Lys23
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 78 kDa.
  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: 111-122 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: 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 with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Cyno/Rhesus Osteoactivin/GPNMB Fc 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 94% aa identity between human and cynomolgus monkey Osteoactivin.  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).

1. Bachner, D. et al. (2002) Gene Exp. Patterns 1:159.
2. Safadi, F.F. et al. (2002) J. Cell. Biochem. 84:12.
3. Ripoll, V.M. et al. (2007) J. Immunol. 178:6557. 
4. Owen, T.A. et al. (2003) Crit. Rev. Eukaryot. Gene Expr. 13:205. 
5. Weterman, M.A.J. et al. (1995) Int. J. Cancer 60:73. 
6. Kuan, C-T. et al. (2006) Clin. Cancer Res. 12:1970. 
7. Lennerz, V. et al. (2005) Proc. Natl. Acad. Sci. USA 102:16013.
8. Genbank Accession # AAH11595.
9. Abdelmagid, S.M. et al. (2007) J. Cell. Physiol. 210:26.
10. Haralanova-Ilieva, B. et al. (2005) J. Hepatol. 42:565.
11. Ahn, J.H. et al. (2002) Blood 100:1742.
12. Anderson, M.G. et al. (2002) Nat. Genet. 30:81.
13. Shikano, S. et al. (2001) J. Biol. Chem. 276:8125.

Bioinformatics

• Uniprot:
  • XP_005550047.1()