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Sialic acid-binding Ig-like lectin 5 is a protein that in Cynomolgus is encoded by the SIGLEC5 gene, Cynomolgus SIGLEC5 cDNA encodes 551 amino acids (aa) that include a 16 aa signal sequence, a 439aa extracellular domain (ECD) with three Ig-like domains, a transmembrane region and a cytoplasma tail. 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. Siglec5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
10 μg | $184 | 7-10 days | |
50 μg | $545 | 7-10 days | |
500 μg | $1,900 | 7-10 days | |
1 mg | $2,970 | 7-10 days |
Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | Sialic acid-binding Ig-like lectin 5 is a protein that in Cynomolgus is encoded by the SIGLEC5 gene, Cynomolgus SIGLEC5 cDNA encodes 551 amino acids (aa) that include a 16 aa signal sequence, a 439aa extracellular domain (ECD) with three Ig-like domains, a transmembrane region and a cytoplasma tail. 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. Siglec5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. |
Species | Cynomolgus |
Expression System | HEK293 Cells |
Tag | C-6xHis |
Accession Number | A0A0B4J1D1 |
Synonyms | Siglec-5,Sialic acid-binding Ig-like lectin 5 |
Amino Acid | Glu17-Gly435 |
Construction | Glu17-Gly435 |
Protein Purity | Greater than 90% as determined by reducing SDS-PAGE. (QC verified) |
Molecular Weight | 90 KDa (reducing condition) |
Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 8.0. |
Reconstitution | Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing. |
Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
Research Background | Sialic acid-binding Ig-like lectin 5 is a protein that in Cynomolgus is encoded by the SIGLEC5 gene, Cynomolgus SIGLEC5 cDNA encodes 551 amino acids (aa) that include a 16 aa signal sequence, a 439aa extracellular domain (ECD) with three Ig-like domains, a transmembrane region and a cytoplasma tail. 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. Siglec5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. |
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