E. coli expression service

The study of proteins or their applications in biotechnological contexts often requires their individual isolation. Methods for purifying proteins from natural sources are typically cumbersome and inefficient for most individuals. Escherichia coli, due to its rapid growth, ease of handling, and cost-effectiveness, has become the preferred host for recombinant protein production. Today, many commercially valuable proteins are produced in Escherichia coli, simultaneously, in the laboratory, E. coli recombinant expression of proteins is the preferred method for studying their structure and function.


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Our E. coli expression platform has gathered various N and C-terminal tags, as well as a variety of expression vectors tailored for different host strains, ensuring the selection of the most effective system and expression scheme.

Platform features
Cost-effective
Cost-effective

Rapid expression with short cultivation time and easy operation

Easy to scale up production
Easy to scale up production

Fermentation for large-scale production with minimal batch variations

Mature system
Mature system

Clearly designed genetic background, streamlined operational procedures

Testing conditions
Testing conditions

Cultivation temperature, induction conditions; host selection, and tag design

Data
Data

SDS-PAGE, WB analysis for quality control, Nanodrop quantification

Service Content

Cycle

Survey
Survey

Preliminary research conducted

1 day
Designing
Designing

Drafting the initial expression strategy, determining tags, vectors, and expression cell lines……

1 day
Expression
Expression

Gene synthesis, vector construction, testing expression and purification conditions

2-3 weeks
Scale-up production
Scale-up production

Determine the production volume based on demand

1-2 weeks
Delivery
Delivery

Experimental reports, cloning vectors, recombinant proteins

1 day
Case Show
Target protein A

Target protein A is a cell validation factor protein.

The full-length segment was chosen as the target fragment for recombinant expression. Codon optimization was performed and integrated into the expression vector. A 6His tag was used, and the expression was carried out in BL21 host cells following transformation with the recombinant construct.

Target protein A
Please feel free to contact us for more information or a detailed quote！