Recombinant Human Osteoactivin/GPNMB Fc Avi-tag Protein, CF Summary
Accession # NP_002501.1
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Recombinant Human Osteoactivin/GPNMB Fc Chimera Avi-tag Protein (Catalog # AVI2550) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 110-126 kDa and 220-250 kDa, respectively.
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).Our Avi-tag Biotinylated Human Osteoactivin/GpNMB Fc chimera protein features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Bachner, D. et al. (2002) Gene Exp. Patterns 1:159.
- Safadi, F.F. et al. (2002) J. Cell. Biochem. 84:12.
- Ripoll, V.M. et al. (2007) J. Immunol. 178:6557.
- Owen, T.A. et al. (2003) Crit. Rev. Eukaryot. Gene Expr. 13:205.
- Weterman, M.A.J. et al. (1995) Int. J. Cancer 60:73.
- Kuan, C-T. et al. (2006) Clin. Cancer Res. 12:1970.
- Lennerz, V. et al. (2005) Proc. Natl. Acad. Sci. USA 102:16013.
- Genbank Accession # AAH11595.
- Abdelmagid, S.M. et al. (2007) J. Cell. Physiol. 210:26.
- Haralanova-Ilieva, B. et al. (2005) J. Hepatol. 42:565.
- Ahn, J.H. et al. (2002) Blood 100:1742.
- Anderson, M.G. et al. (2002) Nat. Genet. 30:81.
- Shikano, S. et al. (2001) J. Biol. Chem. 276:8125.
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