Anti-SIGLEC10, clone SIGLEC10/7582

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Siglec-10 (sialic acid-binding Ig-like lectin 10) is a 697 amino acid protein belonging to the immunoglobulin superfamily. The N-terminal Ig-like domain of Siglec-10 contains a sialic acid-binding site and the C-terminal cytoplasmic region of Siglec-10 contains two immunoreceptor tyrosine-based inhibitor motifs (ITIMs), which are involved in the modulation of cellular responses through SH2 domains. With most expression in spleen, bone marrow and peripheral blood lymphocytes, such as monocytes, natural killer cells and eosinophils, it is likely that Siglec-10 functions as an inhibitory receptor in the immune response. Importantly, Siglec-10 mRNA is found to be highly upregulated in eosinophils at sites of inflammation in asthmatics, suggesting that Siglec-10 may be an appropriate target for new approaches of immunomodulatory therapy. There are six named isoforms of Siglec-10 that are a result of alternative splicing. All isoforms exists as single-pass transmembrane proteins, except for isoform 6, which is secreted. Protein function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (PubMed:11284738, PubMed:12163025). Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1. In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (PubMed:25450598). Plays a role in the control of autoimmunity. During initiation of adaptive immune responses by CD8- alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification. [The UniProt Consortium]