Publications by authors named "Viktoriia A Fridman"
Article Synopsis
- Researchers are developing new strategies to improve the production and purification of recombinant proteins in plants by optimizing gene codon composition and exploring regulatory sequences.
- A case study on interferon-αA demonstrated that using a thermostable protein stabilizer (lichenase) significantly enhances the yield of recombinant proteins without negatively affecting their biological activity.
- The combination of protein stabilization and methods for purifying fusion proteins leads to efficient and cost-effective approaches for producing valuable proteins in plant systems.
Background: Since the beginning of the use of reporter proteins for expression analysis, a variety of approaches have been developed and proposed; both qualitative and quantitative. The lack of simple methods for direct observation of gene expression in living organisms makes it necessary to continue to propose new methods. In this work, we consider a method for the quantitative analysis of the expression of thermostable lichenase from Clostridium thermocellum used as a sensitive reporter protein.
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