Yeast Expression and Purification is often used for structural studies. It is useful when creating proteins that would be toxic in E. coli because yeast cells do not create detectable endotoxins. Yeast cells allow the formation of disulfide bonds which allows for glycosylation. However, this glycosylation does not mimic mammalian cells.
|- Sub-cloning into yeast expression system
- Transient expression and purification
- Stable Cell line establishment
‐ QC testing: SDS-PAGE and protein concentration
|- Weekly progress reports
- Desired quantity of purified, soluble protein
- QC data
|14-19 weeks||Varies with project, please Inquire.|
Western Blot data available FREE of charge for any tagged proteins than can be detected by the anti-HIS antibody. Additional charges apply for all other proteins.