A recombinant partial protein sequence (within amino acids 500-697) from the human protein was used as the immunogen for the SIGLEC10 antibody.
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.
