Siglec-10 Protein, Human (Biotinylated, HEK293, His-Avi)

Siglec-10 protein, recognized as a putative adhesion molecule, functions in sialic-acid dependent cellular binding, displaying a preference for alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site of Siglec-10 may undergo masking due to cis interactions with sialic acids on the same cell surface. In immune responses, it appears to act as an inhibitory receptor, inducing ligand-induced tyrosine phosphorylation and recruiting cytoplasmic phosphatases via their SH2 domains, blocking signal transduction through dephosphorylation of signaling molecules. Siglec-10 is involved in the negative regulation of B-cell antigen receptor signaling, dependent on PTPN6/SHP-1. In association with CD24, it may participate in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70, and HSP90. Siglec-10, in collaboration with CD24, regulates the immune response of natural killer (NK) cells and plays a role in the control of autoimmunity. During the initiation of adaptive immune responses by CD8-alpha(+) dendritic cells, Siglec-10 inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes, implicating the recruitment of PTPN6/SHP-1 and promoting phagosomal acidification. Siglec-10 interacts with various proteins, including PTPN6/SHP-1, NCF1, CD24, HMGB1, RIGI, CBL, and PTPN11.