Recombinant Mouse Siglec-1 Fc Chimera Protein, CF

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5610-SL-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Mouse Siglec-1 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
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 #
N-terminal Sequence
Analysis
Thr20
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
201.7 kDa (monomer)
SDS-PAGE
190-205 kDa under reducing conditions

Product Datasheets

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5610-SL

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

5610-SL

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: Siglec-1/CD169

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).

References
  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.
Long Name
Sialic Acid Binding Ig-like Lectin 1
Entrez Gene IDs
6614 (Human); 20612 (Mouse); 311426 (Rat)
Alternate Names
CD169; FLJ00051; sialic acid binding Ig-like lectin 1, sialoadhesin; sialoadhesin; Siglec1; Siglec-1

Citations for Recombinant Mouse Siglec-1 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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  1. Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1.
    Authors: Chen, Guo-Yun, Brown, Nicholas, Wu, Wei, Khedri, Zahra, Yu, Hai, Chen, Xi, van de Vlekkert, Diantha, D'Azzo, Alessand, Zheng, Pan, Liu, Yang
    Elife, 2014-09-03;3(0):e04066.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Bioassay
  2. The role of Siglec-1 and SR-BI interaction in the phagocytosis of oxidized low density lipoprotein by macrophages.
    Authors: Xiong, Yi-song, Yu, Juan, Li, Chang, Zhu, Lin, Wu, Li-juan, Zhong, Ren-qian
    PLoS ONE, 2013-03-08;8(3):e58831.
    Species: Mouse
    Sample Types: Protein
    Applications: Bioassay

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