Recombinant Human Siglec-9 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 10.0-100 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Siglec-9 protein
>97%, 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
62.7 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
Publications
Read Publications using 1139-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
>97%, 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-9 Fc Chimera Protein, CF
CD329
CDw329
FOAP-9
OBBP-Like
Protein FOAP-9
sialic acid binding Ig-like lectin 9
sialic acid-binding Ig-like lectin 9
Siglec9
Siglec-9
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 Siglec-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.
The cDNA of human Siglec-9 encodes a 463 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-likeV-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail (5, 6). In peripheral blood leukocytes, Siglec-9 is expressed on neutrophils, monocytes, a fraction of NK cells, B cells, and a minor subset of CD8+ T cells (5). It binds equally well to both 2,3- and 2,6-linked sialic acid (5, 6). Siglec-9 is closely related to Siglec-7, and they share ~80% amino acid sequence identity. The gene encoding siglec-9 was mapped to chromosome 19q13.4.
Crocker, P.R. et al. (1998) Glycobiology 8:v.
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.
Zhang, J.Q. et al. (2000) J. Biol. Chem. 275:22121.
Angata, T. et al. (2000) J. Biol. Chem. 275:22127.
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