>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Neu5Ac(a2-6)GalNAc-PAA-biotin is immobilized onto a Streptavidin-coated plate, Recombinant Human Siglec-15 Fc Chimera binds with an ED50 of 150-900 ng/mL.
When Neu5Ac(a2-6)GalNAc-PAA-biotin is immobilized onto aStreptavidin-coated plate, Recombinant Human Siglec-15 Fc Chimera (Catalog # 9227-SL) bindswith an ED50 of 150-900 ng/mL.
Siglec-15 is a transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules (1). Mature human Siglec-15 consists of a 244 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 44 aa cytoplasmic domain (2). Within the ECD, human Siglec-15 shares 85% aa sequence identity with mouse and rat Siglec-15. Alternative splicing generates an additional isoform that lacks the signal peptide and first Ig-like domain. Siglec-15 associates with the signaling molecules DAP12 and DAP10 (2-5). It is expressed on osteoclasts, macrophages, and dendritic cells (2-6) and binds to the sialyl-Tn antigen (2, 3, 6). This interaction induces the production of TGF-beta by tumor-associated macrophages (3). Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts (4-6).