Siglec-10 Protein, Human, Recombinant (hFc & Avi), Biotinylated

1. Loaded Human Siglec-10-Fc-Avi on SA Biosensor, can bind Anti-Human Siglec-10 mAb-Fc with an affinity constant of <10^-3 nM as determined in BLI assay. (Regularly tested) 2. Immobilized Anti-Human Siglec10 mAb at 1μg/ml (100 μl/well) can bind Biotinylated Human Siglec-10-Fc-Avi The ED50 of Biotinylated Human Siglec-10-Fc-Avi is 1.45 ng/ml. (Regularly tested)

Siglec-10 Protein, Human, Recombinant (hFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-Fc-Avi tag. The predicted molecular weight is 100-130 KDa and the accession number is Q96LC7.

Human

HEK293 Cells

Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by a varying number of Ig-like C2-type domains. Siglecs 5-11 constitute the CD33/Siglec-3 related group, and are differentially expressed in the hematopoietic system. Siglec-G is the apparent ortholog of human Siglec-10. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. Siglec-10 binds sialated proteins and lipids in alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides. This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell. When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.