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 calls 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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
IFIHCELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Siglec-10 of human origin by IF IHC(P) and ELISA
Tissue Specificity
recommended for detection of Siglec-10 of human origin by IF, IHC(P) and ELISA