>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.01 EU per 1 μg of the protein by the LAL method.
201.7 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Siglecs are sialic acid specific I-type lectins that belong to the immunoglobulin superfamily. Structurally, they are transmembrane proteins with an N-terminal Ig-like V-set domain followed by varying numbers of Ig-like C2-set domains (1, 2). Mouse Siglec-1, also known as sialoadhesin and CD169, is a 175 - 185 kDa glycoprotein that consists of a 1619 amino acid (aa) extracellular domain (ECD) with one Ig-like V-set domain and 16 Ig‑like C2-set domains, a 21 aa transmembrane segment, and a 35 aa cytoplasmic domain (3, 4). Within the ECD, mouse Siglec-1 shares 73% and 83% aa sequence identity with human and rat Siglec-1, respectively. Alternate splicing generates a soluble form of the ECD and a soluble isoform that is truncated following the first three Ig-like domains (3). Siglec-1 expression is restricted to lymph node and spleen macrophages and some tissue macrophages (4). The adhesive function of Siglec-1 is supported by the N-terminal Ig-like domain which shows a selectivity for alpha -2,3-linked sialic acid residues (4 - 6). Siglec-1 binds a number of sialylated molecules including the mannose receptor, MGL1, MUC1, PSGL-1, and different glycoforms of CD43 (7 - 10). Its binding capacity can be masked by endogenous sialylated molecules (11, 12). The sialylated and sulfated N-linked carbohydrates that modify Siglec-1 itself are required for ligand binding (7, 8). Siglec-1 is expressed on dendritic cells following rhinovirus exposure, and these DC promote T cell anergy (13). It is also induced on circulating monocytes during systemic sclerosis and HIV-1 infection (14 - 16). Siglec-1 can trap HIV-1 particles for trans infection of permissive cells (15).
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13. Kirchberger, S. et al. (2005) J. Immunol. 175:1145.
14. York, M.R. et al. (2007) Arthritis Rheum. 56:1010.
15. Rempel, H. et al. (2008) PloS ONE 3:e1967.
16. van der Kuyl, A.C. et al. (2007) Plos ONE 2:e257.
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