An expert service for your protein requirements
In a landscape where protein-based research is pivotal, our Protein Expression & Purification solution in the E. coli host stands as a beacon of innovation, empowering scientists, researchers, and industries to unlock new frontiers in biotechnology, medicine, and beyond. Welcome to a future where protein expression and purification challenges are met with cutting-edge solutions that redefine what’s achievable.
What sets our solution apart is its adaptability to diverse protein types, from enzymes to therapeutic proteins, and its compatibility with various downstream analyses. Researchers and industries now have a robust tool at their disposal to accelerate drug discovery, protein engineering, and fundamental research, all while maintaining the highest standards of quality and reproducibility.
All we need is the sequence of your protein.
Deliverables
Cloning into vector of your choice with markers.
Deliverables
Transformation, bacterial expression and purification.
Deliverables
Purified protein to be shipped in the formulation buffer.
Deliverables
Your questions answered
E. coli is a well-established and cost-effective host organism for recombinant protein production due to its rapid growth, ease of genetic manipulation, and abundant expression systems.
The process generally involves gene cloning, transformation of E. coli cells, induction of protein expression, cell harvest, cell lysis, purification using chromatography or other methods, and analysis of the purified protein.
Protein purification services can include affinity chromatography, ion-exchange chromatography, size exclusion chromatography, and more, tailored to specific protein properties.
Expression vectors contain a promoter, ribosome binding site, selectable marker, and cloning sites. The gene of interest is inserted to allow controlled protein expression.
Inclusion bodies are aggregates of misfolded proteins that can form during overexpression in E. coli. They often require denaturation, solubilization, and refolding steps during purification.
E. coli lacks some eukaryotic post-translational modification machinery, limiting its ability to produce proteins with certain modifications (e.g., glycosylation).
Challenges include low yields, formation of inclusion bodies, purification of insoluble proteins, and potential contamination with host cell components.
Purity can be evaluated using techniques such as SDS-PAGE, western blotting, and mass spectrometry, while quality may involve functional assays or crystallization studies.
Codon optimization adjusts the gene sequence to match preferred E. coli codons, potentially improving translation efficiency and protein expression levels.
Protein production can range from milligrams to grams per liter of culture, depending on the expression system and protein characteristics.
Project duration can vary widely depending on protein complexity, expression levels, purification requirements, and the chosen protocol, but it can range from weeks to months.
Yes, molecular chaperones and refolding techniques can be employed to aid proper protein folding post-purification. Note that there will be additional charges for this which is generally not included in the quote. Ask for this separately.
Stability is often maintained by working at low temperatures, using protease inhibitors, and handling the protein gently.
Protein concentration is determined using methods like UV spectroscopy, Bradford assay, or BCA assay.
Consider factors like protein size, complexity, solubility, and downstream applications when selecting an expression system.
