Technologies

Start Your Project Now!

Please note: Our products and services are not intended to be used directly in diagnostic or therapeutic procedures.

Here's how you can reach us...

Tel:
Email:

E. coli Expression Technology

Inquiry

Escherichia coli (E. coli) is one of the most widely used expression systems for producing recombinant proteins. CD Formulation integrates E. coli expression technology into our internal protein production platform, offering the ultimate solution for your protein production. We provide a one-stop service from codon optimization to recombinant protein expression and purification.

What is The E. coli Expression Technology?

E. coli, a widely used bacterium, has been recognized by drug regulatory agencies and can grow rapidly to high cell density on cheap carbon sources. It is one of the main expression systems for producing recombinant proteins, such as human proteins (insulin, and interferon) and vaccine antigens. This system is favored for its rapid growth, simple culture conditions, and low production cost. Typical expression strategies include using strong promoters and suitable expression vectors to increase the expression level of the target protein.

Fig. 1 Cell-free protein expression system by using E. coli crude extract. Fig. 1 A simplified representation of cell-free protein expression system by using E. coli crude extract. (Kachhawaha K, et al., 2023)

Our Services Related to E. coli Expression Technology

With our optimized E. coli expression system, we can efficiently produce high-purity recombinant proteins. Our customized workflows and options can meet the downstream applications of your products. Importantly, our team of scientists can help you solve various problems during protein purification.

Codon Optimization and Gene Synthesis (Optional)

Vector Construction

Clone cDNA into the appropriate expression vector.
Plasmid sequencing and bulk plasmid preparation.

Protein Expression Analysis

E. coli strain transformation.
Protein expression assessment (SDS-PAGE).

Expression and Purification

Small-scale expression, purification, and condition optimization.
QC analysis: SDS-PAGE, UV, etc.

Scalable Expression (Optional)

Protein refolding.
Soluble protein and inclusion body purification.
QC analysis: SDS-PAGE, UV, etc.

Large-scale Expression and Purification (Optional)

A large-scale expression and purification according to the selected appropriate expression conditions.
QC analysis: SDS-PAGE, UV, etc.

Target Protein Identification

Identify the protein using qualitative or quantitative analysis methods.
Purified proteins (can be lyophilized).

General Process of Protein Production Using E. coli Expression Technology

Use competent E. coli cells to obtain DNA sequences.
Integrate DNA into bacterial genome and circularize DNA sequences into plasmids.
Use selectable markers to select transformed E. coli.
Cultivate selected E. coli in appropriate media for large scale.
Isolate and purify intracellular or secreted proteins.

Custom E. coli Expression Services

Therapeutic Protein Production

E. coli is a fast and cost-effective way to produce recombinant proteins. Leverage our innovative E. coli protein expression platform for efficient and safe protein drug production. We provide custom E. coli protein expression services, including codon optimization, gene synthesis, vector construction, protein expression, protein.

Features of Yeast Expression Technology

The growth cycle is short, and high cell density can usually be reached within a few hours, which is conducive to the rapid acquisition of large amounts of recombinant proteins.
Genetic manipulation is relatively simple, and the cloning, expression, and purification processes are easy to achieve.
The transformation efficiency of exogenous DNA is high, and the desired recombinant can be obtained with a high probability.
Unparalleled rapid growth kinetics.
Easy to culture, and expression conditions can be controlled.
High-level expression of various types of recombinant proteins, especially for small proteins and some easily soluble proteins.
Fast and simple transformation of exogenous DNA.

Publication

Published Data

Technology: E. coli Expression Technology

Journal: J Microbiol Biotechnol.

IF: 2.5

Published: 2016

Results:

The authors ingeniously engineered the pPT-GI vector and transformed E. coli JM109 to express propeptide glargine insulin. The biological activity of the transformed E. coli cells expressing in the form of inclusion bodies was restored by refolding. The propeptide was converted into glargine insulin by citraconylation and trypsin cleavage. The enzymatic conversion yield of glargine insulin after citraconylation was increased by 3.2 times compared with that without citraconylation. After the enzymatic reaction, two types of chromatography (ion exchange chromatography and reverse phase chromatography) were used to purify the active glargine insulin. Finally, the production process of high-purity recombinant human glargine insulin and the method of blocking the formation of arginine (B31)-insulin was verified and established based on high-performance liquid chromatography analysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Fig. 2 Glargine insulin structure. Fig. 2 Structure of glargine insulin. (Hwang HG, et al., 2016)

Thanks to our in-house advanced E. coli expression platform, CD Formulation is committed to providing efficient and economical production of therapeutic proteins. Please feel free to contact us if you are interested in our services. Learn how our E. coli expression technology can support your recombinant protein synthesis projects.

References

Kachhawaha K, Singh S, Joshi K, et al. Bioprocessing of recombinant proteins from Escherichia coli inclusion bodies: insights from structure-function relationship for novel applications. Prep Biochem Biotechnol. 2023;53(7):728-752.
Niazi SK, Magoola M. Advances in Escherichia coli-Based Therapeutic Protein Expression: Mammalian Conversion, Continuous Manufacturing, and Cell-Free Production. Biologics. 2023; 3(4):380-401.
Hwang HG, Kim KJ, Lee SH, et al. Recombinant Glargine Insulin Production Process Using Escherichia coli. J Microbiol Biotechnol. 2016;26(10):1781-1789.

How It Works

STEP 1

Submit a service request describing your specific research or development need.

STEP 2

We'll email you to provide your quote and confirm order details if applicable.

STEP 3

Execute the project with real-time communication, and deliver the final report promptly.

Related Services