Recombinant Rat B7-H6/NCR3LG1 Protein (His Tag) | PKSR030135

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SKU:
575-PKSR030135
Weight:
1.00 KGS
€794.00
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Description

Recombinant Rat B7-H6/NCR3LG1 Protein (His Tag) | PKSR030135 | Gentaur US, UK & Europe Disrtribition

Synonyms: B7H6

Active Protein: N/A

Activity: A DNA sequence encoding the rat NCR3LG1 (XP_006223356.1) (Met1-Ser308) was expressed with a polyhistidine tag at the C-terminus.

Protein Construction: A DNA sequence encoding the rat NCR3LG1 (XP_006223356.1) (Met1-Ser308) was expressed with a polyhistidine tag at the C-terminus.

Fusion Tag: C-His

Species: Rat

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg protein as determined by the LAL method.

Stability and 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.

Molecular Mass: 35.1 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

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.

Research Area: N/A

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