Recombinant Human Siglec-6/CD327 Protein
Beta LifeScience
SKU/CAT #: BLK-00959P-100UG

Human Siglec-6 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.
Recombinant Human Siglec-6/CD327 Protein
Beta LifeScience
SKU/CAT #: BLK-00959P-100UG
Collections: All products, High-quality recombinant proteins
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 Human Siglec-6/CD327 Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus.It contains Gln27-Val331. |
Purity | > 95% as determined by Tris-Bis PAGE |
Accession | O43699 |
Target Symbol | siglec-6 |
Synonyms | CD327; CD33 antigen-like 1; CD33L1; CDw327; OB-BP1; Siglec-6; SIGLEC6; CD33L; OBBP1 |
Species | Human |
Expression System | HEK293 |
Tag | C-His-Avi |
Expression Range | Gln27-Val331 |
Mol. Weight | The protein has a predicted MW of 36.6 kDa. Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result. |
Form | Lyophilized |
Formulation | Lyophilized from 0.22um filtered solution in PBS (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 that belong 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.Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds to 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. |