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

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

Recombinant Human Siglec-7/CD328 Fc Chimera 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 0.5‑2 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 #: Q9Y286
• N-terminal Sequence: No results obtained: Gln19 predicted
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: SIGLEC7
• Purity: >85%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 64 kDa (monomer).
  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: 90-100 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 and NaCl.
• Purity: >85%, by SDS-PAGE under reducing conditions and visualized by silver stain
• 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-7/CD328 Fc Chimera Protein, CF

• 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

Background

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.

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.

Publications for Siglec-7/CD328 (1138-SL)(8)

Publications using 1138-SL

• 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; Siglec-7 glyco-immune binding mAbs or NK cell engager biologics induce potent antitumor immunity against ovarian cancers Science advances 2023-11-03 [PMID: 37910620] (ICC, Human)
• Chan, C;Lustig, M;Jansen, JHM;Garcia Villagrasa, L;Raymakers, L;Daamen, LA;Valerius, T;van Tetering, G;Leusen, JHW; Sialic Acids on Tumor Cells Modulate IgA Therapy by Neutrophils via Inhibitory Receptors Siglec-7 and Siglec-9 Cancers 2023-06-29 [PMID: 37444515] (Bioassay, Human)
• 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; Targeting stromal cell sialylation reverses T cell-mediated immunosuppression in the tumor microenvironment Cell reports 2023-05-05 [PMID: 37167967] (Flow Cytometry, Human)
• M Vijayan, CL Lee, VHH Wong, X Wang, K Bai, J Wu, H Koistinen, M Seppälä, KF Lee, WSB Yeung, EHY Ng, PCN Chiu Decidual glycodelin-A polarizes human monocytes towards a decidual macrophage-like phenotype via siglec-7 J. Cell. Sci., 2020-07-23;0(0):. 2020-07-23 [PMID: 32513821] (Immunoprecipitation, 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)
• Hudak , Jason E, Canham , Stephen, Bertozzi , Carolyn Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion. Nat Chem Biol, 2013-11-24;10(1):69-75. 2013-11-24 [PMID: 24292068] (Flow Cytometry, Human)
• Varchetta S, Brunetta E, Roberto A, Mikulak J, Hudspeth K, Mondelli M, Mavilio D Engagement of Siglec-7 receptor induces a pro-inflammatory response selectively in monocytes. PLoS ONE, 2012-09-28;7(9):e45821. 2012-09-28 [PMID: 23029261] (Binding Assay, Bacteria - E. Coli, C. albicans)
• 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: SIGLEC7
• Uniprot:
  • Q9Y286()