| Description: | Siglec-10 Protein, identified as a putative adhesion molecule, mediates sialic-acid dependent cellular binding, preferring alpha-2,3- or alpha-2,6-linked sialic acid. Its sialic acid recognition site may undergo masking through cis interactions. In immune responses, Siglec-10 acts as an inhibitory receptor, inducing ligand-induced tyrosine phosphorylation, recruiting SH2 domain-containing phosphatases, and negatively regulating B-cell antigen receptor signaling via PTPN6/SHP-1. In collaboration with CD24, it selectively suppresses the immune response to DAMPs, regulates NK cell response, controls autoimmunity, and inhibits cross-presentation during adaptive immune responses by CD8-alpha(+) dendritic cells. Siglec-10 interacts with proteins including PTPN6/SHP-1, NCF1, CD24, HMGB1, RIGI, CBL, and PTPN11. Siglec-10 Protein, Human (R119A, HEK293, His-Avi) is the recombinant human-derived Siglec-10 protein, expressed by HEK293, with C-Avi, C-His labeled tag. The total length of Siglec-10 Protein, Human (R119A, HEK293, His-Avi) is 530 a.a., with molecular weight of 70-90 kDa. |
