Recombinant Human B7-H6 Fc Chimera Biotinylated Protein, CF Summary
Accession # NP_001189368
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 100 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.
B7-H6 is a glycosylated member of the B7 family of immune co‑stimulatory proteins (1, 2). Mature human B7-H6 consists of a 238 amino acid (aa) extracellular domain (ECD) that contains one Ig-like V domain and one Ig-like C1 domain, a 21 aa transmembrane segment, and a 171 aa cytoplasmic domain that contains one ITIM, one SH2, and one SH3 motif (3). Both of the Ig-like domains carry N-linked glycosylation (4). Within the ECD, human B7-H6 shares 99%, 94%, and 87% aa sequence identity with chimpanzee, orangutan, and gibbon B7-H6, respectively, and 53% - 56% with bovine, canine, and equine B7-H6. Orthologs in mouse and rat have not been identified. The Ig-like V domain mediates 1:1 stoichiometric binding of B7-H6 to NKp30 expressed on NK cells (4, 5). It does not show binding to NKp44, NKp46, or NKG2D (3, 6). Ligation of NKp30 by B7-H6 induces NK cell activation and target cell cytolysis (3). B7-H6 is expressed on a wide range of hematopoietic, carcinoma, and melanoma tumor cells, which is consistent with the detection of NKp30 binding sites on many tumors (3, 7). The expression of NKp30 ligands on tumor cells correlates with tumor cell sensitivity to NKp30‑dependent cell lysis (7).
- Zou, W. and L. Chen (2008) Nat. Rev. Immunol. 8:467.
- Bour-Jordan, H. et al. (2011) Immunol. Rev. 241:180.
- Brandt, C.S. et al. (2009) J. Exp. Med. 206:1495.
- Li, Y. et al. (2011) J. Exp. Med. 208:703.
- Joyce, M.G. et al. (2011) Proc. Natl. Acad. Sci. 108:6223.
- Arnon, T.I. et al. (2006) Semin. Cancer Biol. 16:348.
- Byrd, A. et al. (2007) PLoS ONE 2:e1339.
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