Recombinant Human B7-H6 His-tag Avi-tag Protein, CF

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When Recombinant Human NKp30 Fc Chimera (1849-NK) is immobilized at 5 μg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human B7‑H6 His-tag Avi-tag (Catalog # AVI9309) that produces 50% of the ...read more
2 μg/lane of Biotinylated Recombinant Human B7‑H6 His-tag Avi-tag Protein (Catalog # AVI9309) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human B7-H6 His-tag Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human NKp30 Fc Chimera  (Catalog # 1849-NK) is immobilized at 5 μg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human B7‑H6 His-tag Avi-tag (Catalog # AVI9309) that produces 50% of the optimal binding response is 0.10-0.80 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human B7-H6 protein
Human B7-H6
(Asp25-Ser262)
Accession # Q68D85.1
6-His tagAvi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Asp25
Structure / Form
Biotinylated via Avi-tag
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
29 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
50-58 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 100 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 Human B7-H6 His-tag Avi-tag Protein, CF

  • B7 homolog 6
  • B7H6
  • B7-H6
  • DKFZp686I21167
  • DKFZp686O24166
  • NCR3LG1

Background

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 21aa transmembrane segment, and a 171aa 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). Our Avi-tag Biotinylated human B7-H6 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.
  1. Zou, W. and L. Chen (2008) Nat. Rev. Immunol. 8:467.
  2. Bour-Jordan, H. et al. (2011) Immunol. Rev. 241:180.
  3. Brandt, C.S. et al. (2009) J. Exp. Med. 206:1495.
  4. Li, Y. et al. (2011) J. Exp. Med. 208:703.
  5. Joyce, M.G. et al. (2011) Proc. Natl. Acad. Sci. 108:6223.
  6. Arnon, T.I. et al. (2006) Semin. Cancer Biol. 16:348.
  7. Byrd, A. et al. (2007) PLoS ONE 2:e1339.

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