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Recombinant Human Siglec-5 Fc Chimera Protein, CF

Catalog #: 1072-SL
9 Citations Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
1072-SL-050
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Citations (9)
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human Siglec-5 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>90%, 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 1‑4 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human Siglec-5/CD170 protein
Human Siglec-5
(Glu17-Thr434)
Accession # O15389		 IEGRID Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
O15389
N-terminal Sequence
Analysis
Glu17
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
73 kDa (monomer)
SDS-PAGE
100-110 kDa, reducing conditions

Product Datasheets

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1072-SL

Product Datasheet
COA
SDS

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.

1072-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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Siglec-5/CD170

Siglecs (1) (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins (2) belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding (3), followed by varying numbers of Ig-like C2-type domains (1, 4). Eleven human Siglecs have been cloned and characterized (1, 4). They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and the Siglec-5 to 11 (4, 5, 7). To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Siglec-5 to 11 share a high degree of sequence similarity with CD33/Siglec-3 both in their extracellular and intracellular regions. They are collectively referred to as CD33-related Siglecs. One remarkable feature of the CD33-related Siglecs is their differential expression pattern within the hematopoietic system (4, 5). This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their cytoplasma tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system.

Human Siglec-5 cDNA encodes a 551 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, three Ig-like C2-type domains, a transmembrane region and a cytoplasma tail (6). Siglec-5 exists as a disulfide-linked homodimer on the cell surface and is expressed on monocytes, neutrophils and B cells (4, 5, 6). It binds equally well to both alpha 2,3- and alpha 2,6-linked sialic acid (6).

References
  1. Crocker, P.R. et al. (1998) Glycobiology 8:v.
  2. Powell, L.D. et al. (1995) J. Biol. Chem. 270:14243.
  3. May, A.R. et al. (1998) Mol. Cell 1998. 1:719.
  4. Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
  5. Crocker, P.R. et al. (2001) Immunology 103:137.
  6. Cornish, A.L. et al. (1998) Blood 92:2123.
  7. Angata, T. et al. (2002) J. Biol Chem. 277:24466.
Long Name
Sialic Acid Binding Ig-like Lectin 5
Entrez Gene IDs
8778 (Human)
Alternate Names
CD170 antigen; CD170; CD33 antigen-like 2; CD33L2; CD33L2OB binding protein-2; OBBP2; OB-BP2OB-binding protein 2; OBBP2sialic acid-binding Ig-like lectin 5; Obesity-binding protein 2; sialic acid binding Ig-like lectin 5; sialic acid-binding immunoglobulin-like lectin 5; Siglec5; Siglec-5

Citations for Recombinant Human Siglec-5 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.

9 Citations: Showing 1 - 9
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  1. The prognostic impact of SIGLEC5-induced impairment of CD8+ T cell activation in sepsis
    Authors: Lozano-Rodríguez, R;Avendaño-Ortíz, J;Montalbán-Hernández, K;Ruiz-Rodríguez, JC;Ferrer, R;Martín-Quirós, A;Maroun-Eid, C;González-López, JJ;Fàbrega, A;Terrón-Arcos, V;Gutiérrez-Fernández, M;Alonso-López, E;Cubillos-Zapata, C;Fernández-Velasco, M;Pérez de Diego, R;Pelegrin, P;García-Palenciano, C;Cueto, FJ;Del Fresno, C;López-Collazo, E;
    EBioMedicine
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. Sialic Acids on Tumor Cells Modulate IgA Therapy by Neutrophils via Inhibitory Receptors Siglec-7 and Siglec-9
    Authors: Chan, C;Lustig, M;Jansen, JHM;Garcia Villagrasa, L;Raymakers, L;Daamen, LA;Valerius, T;van Tetering, G;Leusen, JHW;
    Cancers
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Alteration of microbiota antibody-mediated immune selection contributes to dysbiosis in inflammatory bowel diseases
    Authors: E Michaud, L Waeckel, R Gayet, R Goguyer-De, B Chanut, F Jospin, K Bathany, M Monnoye, C Genet, A Prier, C Tokarski, P Gérard, X Roblin, N Rochereau, S Paul
    Embo Molecular Medicine, 2022-07-04;0(0):e15386.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  4. Lectin nanoparticle assays for detecting breast cancer-associated glycovariants of cancer antigen 15-3 (CA15-3) in human plasma
    Authors: J Terävä, L Tiainen, U Lamminmäki, PL Kellokumpu, K Pettersson, K Gidwani
    PLoS ONE, 2019-07-25;14(7):e0219480.
    Species: Human
    Sample Types: Natural Protein
    Applications: Bioassay
  5. Soluble Siglec-5 associates to PSGL-1 and displays anti-inflammatory activity
    Sci Rep, 2016-11-28;6(0):37953.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  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. 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
  8. Human Siglec-5 inhibitory receptor and immunoglobulin A (IgA) have separate binding sites in streptococcal beta protein.
    Authors: Nordstrom T, Movert E, Olin AI, Ali SR, Nizet V, Varki A, Areschoug T
    J. Biol. Chem., 2011-07-27;286(39):33981-91.
    Species: Bacteria
    Sample Types: Protein
    Applications: Surface Plasmon Resonance, Western Blot (Detection)
  9. Structural implications of Siglec-5-mediated sialoglycan recognition.
    Authors: Zhuravleva MA, Trandem K, Sun PD
    J. Mol. Biol., 2007-10-11;375(2):437-47.
    Species: Human
    Sample Types: Carbohydrates
    Applications: Surface Plasmon Resonance

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