Open AccessHigh expression level of human epidermal growth factor (hEGF) using a well-designed fusion protein-tagged construct in E. coli
Author(s) -
D Shams,
Mitra Alizadeh,
Siavash Azari,
Seyed Masoud Hosseini,
Setayesh Yasami-Khiabani,
Saeed Samani,
Mohammad Ali Shokrgozar
Publication year - 2019
Publication title -
bratislavské lekárske listy/bratislava medical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 32
eISSN - 1336-0345
pISSN - 0006-9248
DOI - 10.4149/bll_2019_126
Subject(s) - intein , fusion protein , lac operon , expression vector , escherichia coli , microbiology and biotechnology , chemistry , fusion gene , recombinant dna , biology , gene , biochemistry , rna , rna splicing
The study was aimed at design a good fusion construct that would successfully express the recombinant proteins and produce peptides in Escherichia coli. Two different constructs including human epidermal growth factor (hEGF) gene were designed to obtain an efficient expression level of hEGF. The hEGF sequence was inserted in pET32a vector containing thioredoxin (Trx) sequence and modified pET15b vector containing intein and elastin-like polypeptide (ELP).