Recombinant Mouse Siglec-1 Fc Chimera Protein, CF


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Reactivity MuSpecies Glossary
Applications Bioactivity

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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.
Mouse myeloma cell line, NS0-derived mouse Siglec-1/CD169 protein
Mouse Siglec-1
(Thr20 - Arg1639)
Accession # CAM18034
(Glu98 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>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.


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.
190-205 kDa under reducing conditions
Read Publications using
5610-SL in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.


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


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.

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Gene Symbol Siglec1