Expression and production of heterologous proteins in microorganisms by genetic recombination technology is a hot topic in modern biology. At CD BioGlyco, we provide bioactive lectins production from the culture medium. We have a variety of Expression Systems to choose from, only by combining the target lectin's biological activity and the system's advantages. For the bacterial expression systems, we provide the following several different services.
E. coli is the optimal host for producing foreign proteins. This system is well-suited for the functional expression of non-glycosylated proteins. To facilitate the large-scale production of recombinant lectins, we continuously optimize expression conditions and optimize expression in the cytoplasm of E. coli. Various aspects including growth conditions, culture temperature, expression vectors, and proteolysis are adjusted to promote the productivity of the E. coli system.
Fig.1 The flowchart of E. coli recombinant lectin production service. (CD BioGlyco)
Bacillus is a useful bacteria expression system, that mainly contains some Gram-positive bacilli. These bacteria are easily transformed with many phages and plasmids due to their unique genetic properties. Secreting the desired proteins directly into the fermentation medium facilitates easy processing, eliminating the need for cell destruction or chemical treatment techniques.
Tab.1 Advantages of different bacterial expression systems. (CD BioGlyco)
| E. coli expression systems | Bacillus expression systems |
|---|---|
| Rapid expression | Strong secretion with no involvement of intracellular inclusion bodies |
| High yields and high fermentation capacity | Genetically well-characterized systems |
| Ease of culture | Highly developed transformation and gene replacement technologies |
| Mass production fast | Superior growth characteristics |
| Quickly and precisely genome modifications | Metabolically robust |
Paper Title: Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture
Expression System: E. coli
Technologies: N-terminal sequencing, MALDI-TOF, size exclusion chromatography, SDS-PAGE
Journal: Protein Expression and Purification
Published: 2006
Results: By exploring the expression conditions and the technical process, the total amount of hexahistidine tagged-Griffithsin (His-GRFT) was increased by about 45 times increasing the expression of the protein in the soluble fraction. Phenotypic analysis of recombinant His-GRFT revealed that both the glycoprotein 120 binding properties and anti-HIV activity had the same activity as the native extracts. Chromatographic analysis showed that both the recombinant and the native ones existed in solution as homodimers. This study demonstrated the asexual purification of the batch mode of GRFT, which was also easily extended, yielding high-purity proteins with anti-HIV activity indistinguishable from native GRFT.
Fig.2 SDS-PAGE analyses and size-exclusion chromatography of GRFT. (Giomarelli, et al., 2006)
CD BioGlyco has rich experience in Recombinant Lectin Production. Our professional team is skilled in applying a variety of strains. According to the client's needs, select the corresponding expression host. While obtaining the recombinant lectins, we will also provide the corresponding original data and maps. Moreover, we provide the original expression strains and cloned plasmids if desired. Please feel free to contact us.
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