CD160 antigen is a Lipid-anchor that exists as a disulfide-linked homomultimer. CD160 contains one Ig-like V-type domain. The human CD160 precursor is a cysteine-rich; glycosylphosphatidylinositol-anchored protein of 181 amino acids with a single Ig-like domain. It is weakly homologous to KIR2DL4. CD160 is expressed in the spleen; peripheral blood; and small intestine. Its expression is tightly associated with peripheral blood NK cells and CD8 T lymphocytes with cytolytic effector activity. CD160 is a receptor showing broad specificity for both classical and non-classical MHC class I molecules.
Immobilized Human HVEM/TNFRSF14(Cat: PKSM040955) at 10µg/ml(100 ?l/well) can bind Human CD160-His. The ED50 of Human CD160-His is 3.60 ug/ml .
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
Recombinant Human CD160 is produced by our Mammalian expression system and the target gene encoding Ile27-Ser159 is expressed with a 6His tag at the C-terminus.
Purity:
> 90 % as determined by reducing SDS-PAGE.
Mol Mass:
15.8 kDa
AP Mol Mass:
22 kDa
Formulation:
Lyophilized from a 0.2 µm filtered solution of 20mM PB;150mM NaCl;pH7.4.
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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Human CD160 Recombinant Protein (His tag) (RPES5970)The product page for this antibody is being prepared. If you have a question please don't hesitate to get in touch!
Human CD160 Recombinant Protein (hFc Tag)Description:CD160 is an 27 kDa glycoprotein which was initially identified with the monoclonal antibody BY55. Its expression is tightly associated with...
Human CD160 Recombinant Protein (His Tag)Description:CD160 is an 27 kDa glycoprotein which was initially identified with the monoclonal antibody BY55. Its expression is tightly associated with...
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