Recombinant Cynomolgus Sialic acid-binding Ig-like lectin 5/Siglec-5 (C-6His)(Discontinued)
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| Amount : | 50 µg |
| Content : | Lyophilized from a 0.2 µm filtered solution of PBS, pH8.0. |
| AA sequence : | Recombinant Cynomolgus Siglec-5 is produced by our Mammalian expression system and the target gene encoding Glu17-Gly435 is expressed with a 6His tag at the C-terminus. |
| Alternative Name : | Sialic acid-binding Ig-like lectin 5; Siglec-5 |
Source : Human Cells;
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.
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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