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
>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
Dilutions
Bioactivity
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:
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).
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.
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