ArticleSaudi journal of biological sciences2020
Molecular cloning, expression, overproduction and characterization of human TRAIP Leucine zipper protein.
Article in Saudi journal of biological sciences, 2020. 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, 11 citations in OpenAlex.
- Generation of a recombinant version of a biologically active cell-permeant human HAND2 transcription factor from E. coli.Scientific reports · 2022Article
- Identification of Optimal Expression Parameters and Purification of a Codon-Optimized Human GLIS1 Transcription Factor from Escherichia coli.Molecular biotechnology · 2022Article
- Article
- Generation of cell-permeant recombinant human transcription factor GATA4 from E. coli.Bioprocess and biosystems engineering · 2021Article
- Generation of a Recombinant Stem Cell-Specific Human SOX2 Protein from Escherichia coli Under Native Conditions.Molecular biotechnology · 2021Article
- Article
- Soluble expression, purification, and secondary structure determination of human MESP1 transcription factor.Applied microbiology and biotechnology · 2021Article
- Codon Optimization, Cloning, Expression, Purification, and Secondary Structure Determination of Human ETS2 Transcription Factor.Molecular biotechnology · 2020Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TRAIP interacting protein is known as a negative regulator of TNF-induced-nuclear factor, kappa-light-chain-enhancer of activated B cell (NF-κB) by direct interaction with the adaptor protein TRAF2, which inhibits the function of TRAF2 via the RINGCC domain protein. The TRAIP protein is composed of 469 amino acids with an N-terminal RING motif that is followed by a coiled coil (CC) and leucine zipper domain. TRAIP proteins are critical in programmed cell death, cell proliferation and differentiation, and embryonic development. The critical functions of TRAIP together with the molecular inhibitory mechanism effect of TRAIP have been reported by two different studies and have opened up new research into the field of TRAF biology. In this study, we designed different constructs of the Leucine zipper domain to find the over -expressed construct for further studies. We successfully cloned the C-terminal TRAIP containing the leucine zipper domain. In addition, we have over-expressed and purified the TRAIP LZ for their biochemical characterization.
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