Recombinant Human Siglec-3/CD33 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Siglec-3/CD33 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 1‑4 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human Siglec-3/CD33 protein
Human Siglec-3
(Asp18-His259)
(Val257Leu)
Accession # AAA51948
DIEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Asp18
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
CD33
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
53.4 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
67-85 kDa, reducing conditions
Publications
Read Publications using
1137-SL in the following applications:

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.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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-3/CD33 Fc Chimera Protein, CF

  • CD33 antigen (gp67)
  • CD33 antigen
  • CD33 molecule
  • CD33
  • FLJ00391
  • gp67
  • myeloid cell surface antigen CD33
  • p67
  • sialic acid binding Ig-like lectin 3
  • Sialic acid-binding Ig-like lectin 3
  • Siglec3
  • Siglec-3
  • SIGLEC3gp67

Background

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).

  1. Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
  2. Crocker, P.R. and A. Varki (2001) Immunology 103:137.
  3. Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
  4. Simmons, D. and B. Seed (1988) J. Immunol. 141:2797.
  5. Freeman, S.D. et al. (1995) Blood 85:2002.
  6. Taylor, V.C. et al. (1999) J. Biol. Chem. 274:11505.
  7. Ulyanova, T. et al. (1999) Eur. J. Immunol. 29:3440.

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1137-SL
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Publications for Siglec-3/CD33 (1137-SL)(5)

We have publications tested in 4 confirmed species: Human, Rat, N/A, Virus.

We have publications tested in 3 applications: Binding Assay, Bioassay, Surface Plasmon Resonance.


Filter By Application
Binding Assay
(1)
Bioassay
(3)
Surface Plasmon Resonance
(1)
All Applications
Filter By Species
Human
(1)
Rat
(2)
N/A
(1)
Virus
(1)
All Species
Showing Publications 1 - 5 of 5.
Publications using 1137-SL Applications Species
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;3(0):e04066. 2014 [PMID: 25187624] (Bioassay, Human) Bioassay Human
Ishida A, Akita K, Mori Y, Tanida S, Toda M, Inoue M, Nakada H Negative regulation of Toll-like receptor-4 signaling through the binding of glycosylphosphatidylinositol-anchored glycoprotein, CD14, with the sialic acid-binding lectin, CD33. J Biol Chem, 2014;289(36):25341-50. 2014 [PMID: 25059667] (Binding Assay, N/A) Binding Assay N/A
Zou Z, Chastain A, Moir S Siglecs facilitate HIV-1 infection of macrophages through adhesion with viral sialic acids. PLoS ONE, 2011;6(9):e24559. 2011 [PMID: 21931755] (Surface Plasmon Resonance, Virus) Surface Plasmon Resonance Virus
Robak LA, Venkatesh K, Lee H, Raiker SJ, Duan Y, Lee-Osbourne J, Hofer T, Mage RG, Rader C, Giger RJ 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. J. Neurosci., 2009;29(18):5768-83. 2009 [PMID: 19420245] (Bioassay, Rat) Bioassay Rat
Hasegawa Y, Fujitani M, Hata K, Tohyama M, Yamagishi S, Yamashita T Promotion of axon regeneration by myelin-associated glycoprotein and Nogo through divergent signals downstream of Gi/G. J. Neurosci., 2004;24(30):6826-32. 2004 [PMID: 15282288] (Bioassay, Rat) Bioassay Rat

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Bioinformatics

Gene Symbol CD33
Entrez
Uniprot