Siglec-10 Protein, Mouse (HEK293, His)

Siglec-10 Protein, identified as a putative adhesion molecule, serves as a mediator of sialic-acid-dependent binding to cells, with a preference for alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may undergo masking through cis interactions with sialic acids on the same cell surface. In the immune response, Siglec-10 functions as an inhibitory receptor, achieving ligand-induced tyrosine phosphorylation and recruiting cytoplasmic phosphatases via their SH2 domains to block signal transduction through the dephosphorylation of signaling molecules. Notably, it participates in the negative regulation of B-cell antigen receptor signaling, specifically acting on B1 cells to inhibit Ca(2+) signaling, cellular expansion, and antibody secretion. This inhibition is dependent on PTPN6/SHP-1. Siglec-10, in association with CD24, may be involved in selectively suppressing the immune response to danger-associated molecular patterns (DAMPs) and regulating the immune response of natural killer (NK) cells. Furthermore, it plays a role in controlling autoimmunity and, during the initiation of adaptive immune responses by CD8-alpha(+) dendritic cells, inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. Additionally, in the context of microbial infection by RNA viruses, Siglec-10 inhibits RIG-I signaling in macrophages by promoting its CBL-dependent ubiquitination and degradation via PTPN11/SHP-2. The multifaceted roles of Siglec-10 highlight its intricate involvement in diverse cellular processes and immune modulation.