- SynonymVSIG8,C1orf204
- SourceBiotinylated Human VSIG8, Fc,Avitag (VS8-H82F2) is expressed from human 293 cells (HEK293). It contains AA Val 22 - Gly 263 (Accession # NP_001013683.1).Predicted N-terminus: Val 22Request for sequence
- Molecular Characterization
This protein carries a human IgG1 Fc tag at the C-terminus, followed by a Avi tag (Avitag™).
The protein has a calculated MW of 55.5 kDa. The protein migrates as 60-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- BiotinylationBiotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
- Biotin:Protein RatioThe biotin to protein ratio is 0.5-1 as determined by the HABA assay.
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>95% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Biotinylated Human VSIG8, Fc,Avitag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
- BackgroundV-set and immunoglobulin domain containing 8 (VSIG8), also known as C1orf204, is a type I transmembrane protein of the B7 family within the Ig superfamily. VSIG8 was identified from proteomic analysis of human hair shafts. It is expressed in the hair follicle and shaft, superficial layers of the nail matrix, and superficial layers of oral epithelium.
- References
- (1)Rice, R.H., et al., 2010, J. Proteome Res., 9: 6752-6758.
- (2)Lee, Y.J., et al., 2006, Mol. Cell. Proteomics, 5: 789-800.
- (3)Rice, R.H., et al., 2011, J. Invest. Dermatol., 131: 1936-1938.
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