Recombinant Human Siglec-1 Protein, CF

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5197-SL-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (8)
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Recombinant Human Siglec-1 Protein, CF Summary

Product Specifications

Purity
>80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 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 human Siglec-1/CD169 protein
Ser20-Gln1641, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Ser20
Predicted Molecular Mass
173.9 kDa
SDS-PAGE
175 kDa-190 kDa, reducing conditions

Product Datasheets

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5197-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.

5197-SL

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile 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). 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).

References
  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.
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 Human Siglec-1 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.

8 Citations: Showing 1 - 8
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  1. Selective tumor antigen vaccine delivery to human CD169+ antigen-presenting cells using ganglioside-liposomes
    Authors: 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
    Proc Natl Acad Sci U S A, 2020-10-16;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Anti-Siglec-1 antibodies block Ebola viral uptake and decrease cytoplasmic viral entry
    Authors: 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-
    Nat Microbiol, 2019-06-03;0(0):.
    Species: Mouse
    Sample Types: Antibody, Serum
    Applications: ELISA Capture, Surface Plasmon Resonance (SPR
  3. Membrane-wrapped nanoparticles probe divergent roles of GM3 and phosphatidylserine in lipid-mediated viral entry pathways
    Authors: F Xu, A Bandara, H Akiyama, B Eshaghi, D Stelter, T Keyes, JE Straub, S Gummuluru, BM Reinhard
    Proc. Natl. Acad. Sci. U.S.A., 2018-09-06;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  4. The plasma biomarker soluble SIGLEC-1 is associated with the type I interferon transcriptional signature, ethnic background and renal disease in systemic lupus erythematosus
    Authors: 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
    Arthritis Res. Ther., 2018-07-27;20(1):152.
    Applications: ELISA (Standard)
  5. An innovative immunotherapeutic strategy for ovarian cancer: CLEC10A and glycomimetic peptides
    Authors: LL Eggink, KF Roby, R Cote, J Kenneth Ho
    J Immunother Cancer, 2018-04-17;6(1):28.
    Species: Human
    Sample Types: Peptide
    Applications: Binding Assay
  6. 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: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  7. 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: Human
    Sample Types: Protein
    Applications: Bioassay
  8. Siglecs facilitate HIV-1 infection of macrophages through adhesion with viral sialic acids.
    Authors: Zou Z, Chastain A, Moir S
    PLoS ONE, 2011-09-08;6(9):e24559.
    Species: Virus
    Sample Types: Virus
    Applications: Surface Plasmon Resonance

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