Biotinylated Human Siglec-5/CD170 Protein
Beta LifeScience
SKU/CAT #: BLK-01115P-100UG

Biotinylated Human Siglec-5 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.
Biotinylated Human Siglec-5/CD170 Protein
Beta LifeScience
SKU/CAT #: BLK-01115P-100UG
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Biotinylated Human Siglec-5/CD170 Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus.It contains Glu17-Thr434. |
Purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by SEC-HPLC |
Accession | O15389 |
Target Symbol | Siglec-5/CD170 |
Species | Human |
Expression System | HEK293 |
Tag | C-His-Avi |
Expression Range | Glu17-Thr434 |
Mol. Weight | The protein has a predicted MW of 49.3 kDa. Due to glycosylation, the protein migrates to 70-80 kDa based on Tris-Bis PAGE result. |
Form | Lyophilized |
Formulation | Lyophilized from 0.22 um filtered solution in PBS, 350mM NaCl (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization. |
Endotoxin | Less than 1EU per ug by the LAL method. |
Storage | Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. |
Shipping | Shipped at ambient temperature. |
Gene 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. Siglec 5 is 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. |