Recombinant Human Siglec-3/CD33 Fc Chimera Protein, CF Summary
Accession # AAA51948
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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.
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.
|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.
Siglecs (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 - 3). 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 (1, 2). 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-3 is alternatively known as myeloid cell surface antigen CD33 and GP67. Human Siglec-3 cDNA encodes a 364 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, one Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail (1, 4). Siglec-3 expression is restricted to cells of myelomonocytic lineage (2). It binds sialic acid preferring alpha 2,3- linkage over alpha 2,6- linkage (5). Studies indicated that Siglec-3 recruits SHP-1 and SHP-2 to its ITIMs (6, 7). When co-crosslinking with Fc gamma R1, Siglec-3 inhibits tyrosine phosphorylation and calcium mobilization, suggesting Siglec-3 can mediate inhibitory signals (7).
- Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
- Crocker, P.R. and A. Varki (2001) Immunology 103:137.
- Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
- Simmons, D. and B. Seed (1988) J. Immunol. 141:2797.
- Freeman, S.D. et al. (1995) Blood 85:2002.
- Taylor, V.C. et al. (1999) J. Biol. Chem. 274:11505.
- Ulyanova, T. et al. (1999) Eur. J. Immunol. 29:3440.
Citations for Recombinant Human Siglec-3/CD33 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.
Citations: Showing 1 - 7
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Siglec-9 defines and restrains a natural killer subpopulation highly cytotoxic to HIV-infected cells
Authors: OS Adeniji, L Kuri-Cerva, C Yu, Z Xu, M Ho, GM Chew, C Shikuma, C Tomescu, AF George, NR Roan, LC Ndhlovu, Q Liu, K Muthumani, DB Weiner, MR Betts, H Xiao, M Abdel-Mohs
PloS Pathogens, 2021;17(11):e1010034.
Sample Types: Recombinant Proteins
Applications: Western Blot Control
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;14(7):e0219480.
Sample Types: Natural Protein
Negative regulation of Toll-like receptor-4 signaling through the binding of glycosylphosphatidylinositol-anchored glycoprotein, CD14, with the sialic acid-binding lectin, CD33.
Authors: Ishida A, Akita K, Mori Y, Tanida S, Toda M, Inoue M, Nakada H
J Biol Chem, 2014;289(36):25341-50.
Sample Types: Protein
Applications: Binding Assay
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
Sample Types: Cell Lysates
Siglecs facilitate HIV-1 infection of macrophages through adhesion with viral sialic acids.
Authors: Zou Z, Chastain A, Moir S
PLoS ONE, 2011;6(9):e24559.
Sample Types: Virus
Applications: Surface Plasmon Resonance
Molecular basis of the interactions of the Nogo-66 receptor and its homolog NgR2 with myelin-associated glycoprotein: development of NgROMNI-Fc, a novel antagonist of CNS myelin inhibition.
Authors: Robak LA, Venkatesh K, Lee H, Raiker SJ, Duan Y, Lee-Osbourne J, Hofer T, Mage RG, Rader C, Giger RJ
J. Neurosci., 2009;29(18):5768-83.
Sample Types: Whole Cells
Promotion of axon regeneration by myelin-associated glycoprotein and Nogo through divergent signals downstream of Gi/G.
Authors: Hasegawa Y, Fujitani M, Hata K, Tohyama M, Yamagishi S, Yamashita T
J. Neurosci., 2004;24(30):6826-32.
Sample Types: Whole Cells
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