Cargando…
High-level Expression and Purification of Active Human FGF-2 in Escherichia coli by Codon and Culture Condition Optimization
BACKGROUND: Basic fibroblast growth factor (bFGF) is a member of a highly conserved superfamily of proteins that are involved in cell proliferation, differentiation, and migration. OBJECTIVES: The objective of this study was to overexpress and purify the high-level active human bFGF in Escherichia c...
Autores principales: | Soleyman, Mohammad Reza, Khalili, Mostafa, Khansarinejad, Behzad, Baazm, Maryam |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Kowsar
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4863364/ https://www.ncbi.nlm.nih.gov/pubmed/27175305 http://dx.doi.org/10.5812/ircmj.21615 |
Ejemplares similares
-
Codon-Optimized Expression and Purification of Truncated ORF2 Protein of Hepatitis E Virus in Escherichia coli
por: Farshadpour, Fatemeh, et al.
Publicado: (2014) -
Expression optimization of recombinant cholesterol oxidase in Escherichia coli and its purification and characterization
por: Fazaeli, Aliakbar, et al.
Publicado: (2018) -
High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli
por: Wang, Huiyan, et al.
Publicado: (2010) -
Improved protein production and codon optimization analyses in Escherichia coli by bicistronic design
por: Nieuwkoop, Thijs, et al.
Publicado: (2018) -
Codon-Optimized Rhodotorula glutinis PAL Expressed in Escherichia coli With Enhanced Activities
por: Xue, Feiyan, et al.
Publicado: (2021)