ArticleBioprocess and biosystems engineering2021
Generation of cell-permeant recombinant human transcription factor GATA4 from E. coli.
Article in Bioprocess and biosystems engineering, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Production of Bioactive Human PAX4 Protein from E. coli.The protein journal · 2023Article
- Biological activity of recombinant human PDX1 protein produced from Escherichia coli.Journal of biochemical and molecular toxicology · 2023Article
- Direct Cardiac Reprogramming: Current Status and Future Prospects.Advances in experimental medicine and biology · 2023Review
- Generation of a recombinant version of a biologically active cell-permeant human HAND2 transcription factor from E. coli.Scientific reports · 2022Article
- Pex30 undergoes phosphorylation and regulates peroxisome number in Saccharomyces cerevisiae.Molecular genetics and genomics : MGG · 2022Article
- Identification of Optimal Expression Parameters and Purification of a Codon-Optimized Human GLIS1 Transcription Factor from Escherichia coli.Molecular biotechnology · 2022Article
- Protein Production and Purification of a Codon-Optimized Human NGN3 Transcription Factor from E. coli.The protein journal · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Transcription factor GATA4 is expressed during early embryogenesis and is vital for proper development. In addition, it is a crucial reprogramming factor for deriving functional cardiomyocytes and was recently identified as a tumor suppressor protein in various cancers. To generate a safe and effective molecular tool that can potentially be used in a cell reprogramming process and as an anti-cancer agent, we have identified optimal expression parameters to obtain soluble expression of human GATA4 in E. coli and purified the same to homogeneity under native conditions using immobilized metal ion affinity chromatography. The identity of GATA4 protein was confirmed using western blotting and mass spectrometry. Using circular dichroism spectroscopy, it was demonstrated that the purified recombinant protein has maintained its secondary structure, primarily comprising of random coils and α-helices. Subsequently, this purified recombinant protein was applied to human cells and was found that it was non-toxic and able to enter the cells as well as translocate to the nucleus. Prospectively, this cell- and nuclear-permeant molecular tool is suitable for cell reprogramming experiments and can be a safe and effective therapeutic agent for cancer therapy.
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Registered trials
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