Recombinant Cynomolgus SIGLEC5/CD170 Protein (His Tag) | PKSQ050010

Recombinant Cynomolgus SIGLEC5/CD170 Protein (His Tag) | PKSQ050010 | Gentaur US, UK & Europe Disrtribition

Synonyms: Sialic acid-binding Ig-like lectin 5; Siglec-5; CD170;CD33L2;OB-BP2;OBBP;OBBP2;SIGLEC-5;SIGLEC5

Active Protein: N/A

Activity: Recombinant Cynomolgus SIGLEC5 is produced by our Mammalian expression system and the target gene encoding Glu17-Gly435 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Cynomolgus SIGLEC5 is produced by our Mammalian expression system and the target gene encoding Glu17-Gly435 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-His

Species: Cynomolgus

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 46.8 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH8.0.

Reconstitution: Please refer to the printed manual for detailed information.

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.

Research Area: N/A