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|Starting Material:||Plasmid||Starting Information:||Sequences Of Target Protein|
|Deliverables:||Cloning Vector||Report:||QC Data|
Protein Refolding Protein Expression Purification,
5mg Soluble Protein Expression Purification
E.coli is the preferential one of bacterial systems for recombinant protein production and large scale fermentation as its advantages including fast rate of reproduction, ease of culture, and rich knowledge about its genetics. Bacterial protein expression service offered by CELLFREE provide a relatively simple, fast, and inexpensive platform for native and heterologous recombinant protein production.
|Plasmids or sequences of target protein||
The eukaryotic protein expressed in E. coli may form the inactive aggregates of protein known as inclusion bodies. Using our unique bio-informatics software MaxcodonTM, we can reduce the chance of the formation of inclusion bodies in expression process.
If the expressed recombinant proteins aggregate into the form of inclusion bodies, the first step of refolding is washing as inclusion bodies contains some outer membrane proteins, plasmid DNA, etc. The washing buffer is usually carried out by using a lower concentration of denaturant (such as urea) or a mild detergent (such as Triton X-100).
After washing, inclusion bodies need dissolute for refolding. Denaturing agents such as urea and guanidine hydrochloride can break through various chemical bonds between the molecules of inclusion bodies, resulting in dissolution of inclusion bodies.
Generally, the refolding methods mainly include dilution, dialysis, molecular sieve chromatography and ion exchange chromatography. Four different methods have their own advantages and disadvantages. Please contact us for more detailed information.