SIGLEC7
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 85 % as determined by SDS-PAGE and Coomassie blue staining.
SIGLEC7, also known as sialic acid-binding Ig-like lectin 7 isoform 1, is a recently discovered family of sialic acid-binding lectins of the immunoglobulin (Ig) superfamily. The extracellular portion has two Ig-like domains, with the amino-terminal V-set Ig domain including amino acid residues known to be involved in sialic acid recognition by other Siglecs. The combination of an extracellular sialic acid binding site and an intracellular ITIM motif suggests that this molecule is involved in trans-membrane regulatory signaling reactions. It exists as a monomer on the cell surface and is expressed on natural killer cells. Recombinant human SIGLEC7, fused to hIgG-His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.
Poids moléculaire
64.2kDa (577aa) 70-100kDa (SDS-PAGE under reducing conditions)