Recombinant Mouse Siglec-1 Fc Chimera Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Siglec-1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. Kelm, S. et al. (1994) Current Biology 4:965. The ED₅₀ for this effect is 0.6-3 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse Siglec-1/CD169 protein
  

  Mouse Siglec-1 (Thr20 - Arg1639) Accession # CAM18034	IEGRMDP	Mouse IgG2a (Glu98 - Lys330)
  N-terminus		C-terminus

• Accession #: CAM18034
• N-terminal Sequence: Thr20
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Siglec1
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 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.
• SDS-PAGE: 190-205 kDa under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Siglec-1 Fc Chimera Protein, CF

• CD169
• FLJ00051
• sialic acid binding Ig-like lectin 1, sialoadhesin
• sialoadhesin
• Siglec1
• Siglec-1

Background

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).

1. Varki, A. and T. Angata (2006) Glycobiology 16:1R.
2. Crocker, P.R. et al. (2007) Nat. Rev. Immunol. 7:255.
3. Crocker, P.R. et al. (1994) EMBO J. 13:4490.
4. Hartnell, A. et al. (2001) Blood 97:288.
5. Nath, D. et al. (1995) J. Biol. Chem. 270:26184.
6. Crocker, P.R. et al. (1991) EMBO J. 10:1661.
7. Martinez-Pomares, L. et al. (1999) J. Biol. Chem. 274:35211.
8. Kumamoto, Y. et al. (2004) J. Biol. Chem. 279:49274.
9. Nath, D. et al. (1999) Immunology 98:213.
10. van den Berg, T.K. et al. (2001) J. Immunol. 166:3637.
11. Nakamura, K. et al. (2002) Glycobiology 12:209.
12. Barnes, Y.C. et al. (1999) Blood 93:1245.
13. 13. Kirchberger, S. et al. (2005) J. Immunol. 175:1145.
14. 14. York, M.R. et al. (2007) Arthritis Rheum. 56:1010.
15. 15. Rempel, H. et al. (2008) PloS ONE 3:e1967.
16. 16. van der Kuyl, A.C. et al. (2007) Plos ONE 2:e257.

Publications for Siglec-1/CD169 (5610-SL)(2)

Publications using 5610-SL

• Chen , Guo-Yun, Brown , Nicholas, Wu , Wei, Khedri , Zahra, Yu , Hai, Chen , Xi, van de Vlekkert , Diantha, D'Azzo , Alessand, Zheng , Pan, Liu , Yang Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1. Elife, 2014-09-03;3(0):e04066. 2014-09-03 [PMID: 25187624] (Bioassay, Mouse)
• Xiong , Yi-song, Yu , Juan, Li , Chang, Zhu , Lin, Wu , Li-juan, Zhong , Ren-qian The role of Siglec-1 and SR-BI interaction in the phagocytosis of oxidized low density lipoprotein by macrophages. PLoS ONE, 2013-03-08;8(3):e58831. 2013-03-08 [PMID: 23520536] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: Siglec1
• Uniprot:
  • CAM18034()