Biotinylated Human Siglec-5/CD170 Protein
Catalog No: CD170-HB001
- Species
- Human
- Expression System
- HEK293
- Tag
- His, Avi
Product overview
Recombinant Biotinylated Human Siglec-5/CD170 Protein is expressed in HEK293 cells with a His tag and Avi tag at the C-terminus. It contains amino acid residues Glu17-Thr434 (UniProt accession: O15389).
Product Details
- Molecular Aliases
- CD170; CD33 antigen-like 2; CD33L2; OBBP2; Siglec5; SIGLEC5; OB-BP2
- Protein Length
- Glu17-Thr434
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 49.3 kDa. Due to glycosylation, the protein migrates to 70-80 kDa based on Bis-Tris PAGE result.
- Purity
- > 90% as determined by Bis-Tris PAGE > 90% as determined by HPLC
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22 μm filtered solution in PBS, 350mM NaCl (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display
Biotinylated Human Siglec-5 on Bis-Tris PAGE under reduced condition. The purity is greater than 90%.
The purity of Biotinylated Human Siglec-5 is greater than 90% as determined by SEC-HPLC.
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.
References
- Macauley M S, Crocker P R, Paulson J C. Siglec-mediated regulation of immune cell function in disease[J]. Nature Reviews Immunology, 2014, 14(10):653-666.
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