Mouse Siglec-1/CD169 Antibody Summary
Accession # Q62230
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Mouse Siglec‑1/CD169 by Western Blot. Western blot shows lysates of mouse lymph node tissue. PVDF Membrane was probed with 1 µg/mL of Sheep Anti-Mouse Siglec-1/CD169 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5610) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Siglec-1/CD169 at approximately 180-190 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Cell Adhesion Mediated by Siglec‑1/CD169 and Neutral-ization by Mouse Siglec‑1/CD169 Antibody. Cell Adhesion Mediated by Siglec-1/CD169 and Neutralization by Mouse Siglec-1/CD169 Antibody. Recombinant Mouse Siglec-1/CD169 Fc Chimera (Catalog # 5610-SL), immobilized onto a microplate, supports the adhesion of human red blood cells in a dose-dependent manner (orange line). Adhesion elicited by Recombinant Mouse Siglec-1/CD169 Fc Chimera (5 µg/mL) is neutralized (green line) by increasing concentrations of Sheep Anti-Mouse Siglec-1/CD169 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5610). The ND50is typically 1-5 µg/mL.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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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