ArticleIranian Red Crescent medical journal2016
High-level Expression and Purification of Active Human FGF-2 in Escherichia coli by Codon and Culture Condition Optimization.
Article in Iranian Red Crescent medical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 34 citations in OpenAlex.
- Further characterization and engineering of an 11-amino acid motif for enhancing recombinant soluble protein expression.Microbial cell factories · 2025Article
- Optimization of recombinant neurturin expression in Escherichia coli using response surface methodology.Biotechnology letters · 2025Article
- FGF-2 enriched nanofiber scaffold for advancing achilles tendon healing: a comparative experimental investigation.Frontiers in surgery · 2024Article
- Refined and benchmarked homemade media for cost-effective, weekend-free human pluripotent stem cell culture.Open research Europe · 2024Article
- Scaling up production of recombinant human basic fibroblast growth factor in anFrontiers in pharmacology · 2023Article
- Biomaterial-Based bFGF Delivery for Nerve Repair.Oxidative medicine and cellular longevity · 2023Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
backgroundBasic fibroblast growth factor (bFGF) is a member of a highly conserved superfamily of proteins that are involved in cell proliferation, differentiation, and migration.
objectivesThe objective of this study was to overexpress and purify the high-level active human bFGF in Escherichia coli (E. coli). MATERIALS AND
methodsThis experimental study was conducted in the Islamic Republic of Iran. After codon optimization and gene synthesis, the optimized FGF-2 gene was subcloned into plasmid pET-32a. pET32-FGF-2 was transformed into E. coli BL21 for expression. The cultivation parameters were optimized to produce a high yield of FGF-2.
resultsThe optimal conditions were determined as follows: cultivation at 37°C in TB medium, with 1 mM isopropyl-β-D-thiogalactopyranoside (IPTG), followed by post-induction expression for 6 h. Under the abovementioned conditions, the expression volumetric productivity of FGF-2 reached 1.48 g/L.
conclusionsA fusion tag from the pET32 expression plasmid permits the recovery of the recombinant fusion FGF-2 from E. coli, without affecting its biological activity.
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