Recombinant Human Siglec-1 Protein, CF

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

Recombinant Human Siglec-1 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 human Siglec-1/CD169 protein
  Ser20-Gln1641, with a C-terminal 6-His tag
• Accession #: Q9BZZ2
• N-terminal Sequence: Ser20
• Protein/Peptide Type: Recombinant Proteins
• Gene: SIGLEC1
• Purity: >80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 173.9 kDa.
  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: 175 kDa-190 kDa, 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: >80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human Siglec-1 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). Human Siglec-1, also known as sialoadhesin and CD169, is a 175-185 kDa glycoprotein. It contains a 1622 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 44 aa cytoplasmic domain (3). Within the ECD, human Siglec-1 shares approximately 70% aa sequence identity with mouse and rat Siglec-1. Alternate splicing generates a potentially soluble form of the ECD, and a second isoform with a substituted cytoplasmic domain. Siglec-1 expression is restricted to lymph node and splenic macrophages, plus some tissue macrophages (3). 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 (3-5). Siglec-1 binds a number of sialylated molecules including the mannose receptor, MGL1, MUC1, PSGL-1, and different glycoforms of CD43 (6-9). Its binding capacity can be masked by endogenous sialylated molecules (10, 11). The sialylated and sulfated N-linked carbohydrates that modify Siglec-1 itself are required for ligand binding (6, 7). Siglec-1 is expressed on dendritic cells following rhinovirus exposure, and these DC promote T cell anergy (12). It is also induced on circulating monocytes during systemic sclerosis and HIV-1 infection (13 - 15). Siglec-1 can trap HIV-1 particles for trans infection of permissive cells (14).

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

Publications for Siglec-1/CD169 (5197-SL)(8)

Publications using 5197-SL

• AJ Affandi, J Grabowska, K Olesek, M Lopez Vene, A Barbaria, E Rodríguez, PPG Mulder, HJ Pijffers, M Ambrosini, H Kalay, T O'Toole, ES Zwart, G Kazemier, K Nazmi, FJ Bikker, J Stöckl, AJM van den Ee, TD de Gruijl, G Storm, Y van Kooyk, JMM den Haan Selective tumor antigen vaccine delivery to human CD169+ antigen-presenting cells using ganglioside-liposomes Proc Natl Acad Sci U S A, 2020-10-16;0(0):. 2020-10-16 [PMID: 33067394] (Bioassay, Human)
• D Perez-Zsol, I Erkizia, M Pino, M García-Gal, MT Martin, S Benet, J Chojnacki, MT Fernández-, D Guerrero, V Urrea, X Muñiz-Trab, L Kremer, J Martinez-P, N Izquierdo- Anti-Siglec-1 antibodies block Ebola viral uptake and decrease cytoplasmic viral entry Nat Microbiol, 2019-06-03;0(0):. 2019-06-03 [PMID: 31160823] (ELISA Capture, Surface Plasmon Resonance (SPR, Mouse)
• F Xu, A Bandara, H Akiyama, B Eshaghi, D Stelter, T Keyes, JE Straub, S Gummuluru, BM Reinhard Membrane-wrapped nanoparticles probe divergent roles of GM3 and phosphatidylserine in lipid-mediated viral entry pathways Proc. Natl. Acad. Sci. U.S.A., 2018-09-06;0(0):. 2018-09-06 [PMID: 30190430] (Bioassay, Human)
• JJ Oliveira, S Karrar, DB Rainbow, CL Pinder, P Clarke, A Rubio Garc, O Al-Assar, K Burling, S Morris, R Stratton, TJ Vyse, LS Wicker, JA Todd, RC Ferreira The plasma biomarker soluble SIGLEC-1 is associated with the type I interferon transcriptional signature, ethnic background and renal disease in systemic lupus erythematosus Arthritis Res. Ther., 2018-07-27;20(1):152. 2018-07-27 [PMID: 30053827] (ELISA (Standard))
• LL Eggink, KF Roby, R Cote, J Kenneth Ho An innovative immunotherapeutic strategy for ovarian cancer: CLEC10A and glycomimetic peptides J Immunother Cancer, 2018-04-17;6(1):28. 2018-04-17 [PMID: 29665849] (Binding Assay, Human)
• 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, Human)
• 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, Human)
• Zou Z, Chastain A, Moir S Siglecs facilitate HIV-1 infection of macrophages through adhesion with viral sialic acids. PLoS ONE, 2011-09-08;6(9):e24559. 2011-09-08 [PMID: 21931755] (Surface Plasmon Resonance, Virus)

Bioinformatics

• Gene Symbol: SIGLEC1
• Uniprot:
  • Q9BZZ2(Human)