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.
Siglec-7 is a member of the human CD33-related Siglec receptor. The extracellular region of Siglec-7 is characterized by an N-terminal V-set Ig domain that can bind sialic acid and two C2-set Ig domains. The cytoplasmic tail of Siglec-7 has one immune-receptor tyrosine-based inhibitory motif (ITIM) and one ITIM-like motif. Siglec-7 is considered as a sialic acid-dependent immunoreceptor with inhibitory potential and expressed predominantly on human NK cells, monocytes and a small subset of CD8+ T cells.