Recombinant Human B7-H6 Protein (His Tag)(Active)
SKU: PKSH030461-50
Recombinant Human B7-H6 Protein (His Tag)(Active)
SKU # | PKSH030461 |
Expression Host | HEK293 Cells |
Description
Synonyms | B7-H6, B7H6, DKFZp686O24166 |
Species | Human |
Expression Host | HEK293 Cells |
Sequence | Met 1-Ser262 |
Accession | NP_001189368.1 |
Calculated Molecular Weight | 28.1 kDa |
Tag | C-His |
Bio-activity | Immobilized human B7-H6 -His at 10μg/mL (100μL/well) can bind human NCR3-Fch, the EC50 of human NCR3-Fch is 6-200ng/mL. |
Properties
Purity | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution | Please refer to the printed manual for detailed information. |
Background
Natural cytotoxicity triggering receptor 3 ligand 1(B7-H6) is a glycosylated member of the B7 family of immune costimulatory proteins. 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. Both of the Ig-like domains carry N-linked glycosylation. The Ig-like V domain mediates 1:1 stoichiometric binding of B7-H6 to NKp30 expressed on NK cells. It does not show binding to NKp44, NKp46, or NKG2D. Ligation of NKp30 by B7-H6 induces NK cell activation and target cell cytolysis. 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.