Production of Nα-acetylated thymosin α1 in Escherichia coli
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Summary
The present data demonstrate that Nα-acetylated Tα1 can be efficiently produced in recombinant E. coli and could be used as an alternative to chemosynthesis for the production of T α1.
- Type
- article
- Published
- 2011-04-22
- Cited by
- 21
- References
- 27
- Access
- Open access
- OpenAlex
- https://openalex.org/W2036059451
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:5448055
Keywords
Intein, Escherichia coli, Fusion protein, Acetylation, Biochemistry
References
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- Engineering proteins to facilitate bioprocessing.
- Synthesis of thymosin .alpha.1
- Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli.
- Recombinant thymosin beta 4 can promote full-thickness cutaneous wound healing.
- Gene fusion expression systems in Escherichia coli.
- Isolation of thymosin alpha 1 from thymosin fraction 5 of different species by high-performance liquid chromatography.
- Production of a recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system
- Minimization of a eukaryotic mini-intein.
- Intein-mediated rapid purification of Cre recombinase.
- Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step.
- Biosynthesis of Staphylococcus aureus Autoinducing Peptides by Using the Synechocystis DnaB Mini-Intein
- InBase: the Intein Database
- Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins.
- Production of thymosin α1 via non‐enzymatic acetylation of the recombinant precursor
- Genetics of proteolysis in Escherichia coli*.
Cited by
- Co-expression for intracellular processing in microbial protein production
- Bacterial expression systems for recombinant protein production: E. coli and beyond.
- Generation of Mature Nα-Terminal Acetylated Thymosin α1 by Cleavage of Recombinant Prothymosin α
- Expanding the landscape of recombinant protein production in Escherichia coli
- Selective N-terminal fluorescent labeling of proteins using 4-chloro-7-nitrobenzofurazan: a method to distinguish protein N-terminal acetylation.
- RimJ-mediated context-dependent N-terminal acetylation of the recombinant Z-domain protein in Escherichia coli.
- RimJ-Catalyzed Sequence-Specific Protein N-Terminal Acetylation in Escherichia coli
- Development of the intein-mediated method for production of recombinant thymosin β4 from the acetylated in vivo fusion protein.
- Constructing novel E.coli cell factories by genome engineering
- High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives
- Efficient biosynthesis of a Cecropin A-melittin mutant in Bacillus subtilis WB700
- Production of Nα-acetyl Tα1-HSA through in vitro acetylation by RimJ
- Design of a substrate-tailored peptiligase variant for the efficient synthesis of thymosin-α1.
- Highly effective biosynthesis of N-acetylated human thymosin β4 (Tβ4) in Escherichia coli
- A survival selection strategy for engineering synthetic binding proteins that specifically recognize post-translationally phosphorylated proteins
- Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins
- In Vitro N-Terminal Acetylation of Bacterially Expressed Parvalbumins by N-Terminal Acetyltransferases from Escherichia coli
- Phenotypic drug discovery: a case for thymosin alpha-1
- Aeromonas spp. as a fast-growing high-performance chassis for protein production
- “Probable acetyltransferase” TTHA1209 Thermus thermophilus bacteria: Gene cloning, structural and functional analysis of the enzyme
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