Recombinant Human Siglec-7/CD328 Fc Chimera Protein, CF

Catalog # Availability Size / Price Qty
1138-SL-050
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Recombinant Human Siglec-7/CD328 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>85%, by SDS-PAGE under reducing conditions and visualized by silver stain
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 0.5‑2 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human Siglec-7/CD328 protein
Human Siglec-7
(Gln19-Gly357)
Accession # Q9Y286
DIEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
No results obtained: Gln19 predicted
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
64 kDa (monomer)
SDS-PAGE
90-100 kDa, reducing conditions

Product Datasheets

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1138-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.

1138-SL

Formulation Lyophilized from a 0.2 μm filtered solution in PBS and NaCl.
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-7/CD328

Siglecs (1) (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains (1, 2). Eleven human Siglecs have been cloned and characterized. They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and Siglecs 5 to 11 (1 - 4). 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. Siglecs 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 (2, 3). This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their cytoplasmic tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system.

Human Siglec-7 encodes a 467 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail (5). Siglec-7 exists as a monomer on the cell surface and is expressed on natural killer cells, CD8+ T cells and monocytes (3, 5). It binds equally well to both alpha 2,3- and alpha 2,6-linked sialic acid (5). The gene encoding Siglec-7 was mapped to chromosome 19q13.3.

References
  1. Crocker, P.R. et al. (1998) Glycobiology 8:v.
  2. Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
  3. Crocker, P.R. and A. Varki (2001) Immunology 103:137.
  4. Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
  5. Nicoll, G. et al. (1999) J. Biol. Chem. 274:34089.
Long Name
Sialic Acid Binding Ig-like Lectin 7
Entrez Gene IDs
27036 (Human)
Alternate Names
Adhesion inhibitory receptor molecule 1; adhesion inhibitory receptor molecule 1, siglec-7; AIRM1; AIRM-1; AIRM1QA79 membrane protein; CD328 antigen; CD328; CDw328; D-siglec; p75; p75/AIRM1; QA79; sialic acid binding Ig-like lectin 7; sialic acid binding immunoglobulin-like lectin 7; sialic acid-binding Ig-like lectin 7; Siglec7; Siglec-7

Citations for Recombinant Human Siglec-7/CD328 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.

8 Citations: Showing 1 - 8
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  1. Siglec-7 glyco-immune binding mAbs or NK cell engager biologics induce potent antitumor immunity against ovarian cancers
    Authors: Bordoloi, D;Kulkarni, AJ;Adeniji, OS;Pampena, MB;Bhojnagarwala, PS;Zhao, S;Ionescu, C;Perales-Puchalt, A;Parzych, EM;Zhu, X;Ali, AR;Cassel, J;Zhang, R;Betts, MR;Abdel-Mohsen, M;Weiner, DB;
    Science advances
    Species: Human
    Sample Types: Whole Cells
    Applications: ICC
  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. Targeting stromal cell sialylation reverses T cell-mediated immunosuppression in the tumor microenvironment
    Authors: Egan, H;Treacy, O;Lynch, K;Leonard, NA;O'Malley, G;Reidy, E;O'Neill, A;Corry, SM;De Veirman, K;Vanderkerken, K;Egan, LJ;Ritter, T;Hogan, AM;Redmond, K;Peng, L;Che, J;Gatlin, W;Jayaraman, P;Sheehan, M;Canney, A;Hynes, SO;Kerr, EM;Dunne, PD;O'Dwyer, ME;Ryan, AE;
    Cell reports
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  4. Decidual glycodelin-A polarizes human monocytes towards a decidual macrophage-like phenotype via siglec-7
    Authors: M Vijayan, CL Lee, VHH Wong, X Wang, K Bai, J Wu, H Koistinen, M Seppälä, KF Lee, WSB Yeung, EHY Ng, PCN Chiu
    J. Cell. Sci., 2020-07-23;0(0):.
    Species: Human
    Sample Types: Protein
    Applications: Immunoprecipitation
  5. 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
  6. Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion.
    Authors: Hudak, Jason E, Canham, Stephen, Bertozzi, Carolyn
    Nat Chem Biol, 2013-11-24;10(1):69-75.
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  7. Engagement of Siglec-7 receptor induces a pro-inflammatory response selectively in monocytes.
    Authors: Varchetta S, Brunetta E, Roberto A, Mikulak J, Hudspeth K, Mondelli M, Mavilio D
    PLoS ONE, 2012-09-28;7(9):e45821.
    Species: Bacteria - E. Coli, C. albicans
    Sample Types: Whole Cells
    Applications: Binding Assay
  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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