Facile expression and purification of active human growth hormone in E. coli by a cleavable self-aggregating tag scheme

Engineered small metal‐binding protein tag improves the production of recombinant human growth hormone in the periplasm of Escherichia coli

(2020) David A. Perez‐Perez et al.   FEBS Open Bio

New tools for recombinant protein production in Escherichia coli : A 5-year update

(2019) Germán L. Rosano et al.   PROTEIN SCIENCE

Escherichia coli “TatExpress” strains export several g/L human growth hormone to the periplasm by the Tat pathway

(2019) Isabel Guerrero Montero et al.   BIOTECHNOLOGY AND BIOENGINEERING

Engineered pH‐inducible intein Mtu ΔI‐CM variants with markedly reduced premature cleavage activity

(2019) Zhanglin Lin et al.   AICHE JOURNAL

Recombinant Protein Expression in Escherichia coli (E.coli): What We Need to Know

(2018) Seyed Mohammad Gheibi Hayat et al.   CURRENT PHARMACEUTICAL DESIGN

Strategies for optimization of heterologous protein expression in E. coli : Roadblocks and reinforcements

(2018) Jashandeep Kaur et al.   INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

A cleavable self-assembling tag strategy for preparing proteins and peptides with an authentic N-terminus

(2017) Qing Zhao et al.   Biotechnology Journal

Recombinant production of medium- to large-sized peptides in Escherichia coli using a cleavable self-aggregating tag

(2016) Qing Zhao et al.   Microbial Cell Factories

Thiol-Disulfide Exchange in Human Growth Hormone

(2016) Saradha Chandrasekhar et al.   PHARMACEUTICAL RESEARCH

Advanced technologies for improved expression of recombinant proteins in bacteria: perspectives and applications

(2015) Sanjeev K. Gupta et al.   CRITICAL REVIEWS IN BIOTECHNOLOGY

Cloning, Expression, and Purification of a Synthetic Human Growth Hormone in Escherichia coli Using Response Surface Methodology

(2014) Mozhdeh Zamani et al.   MOLECULAR BIOTECHNOLOGY

Prokaryotic Soluble Overexpression and Purification of Bioactive Human Growth Hormone by Fusion to Thioredoxin, Maltose Binding Protein, and Protein Disulfide Isomerase

(2014) Minh Tan Nguyen et al.   PLoS One

High-level expression and purification of recombinant human growth hormone produced in soluble form in Escherichia coli

(2014) Zdenko Levarski et al.   PROTEIN EXPRESSION AND PURIFICATION

Recombinant protein expression in Escherichia coli: advances and challenges

(2014) Germán L. Rosano et al.   Frontiers in Microbiology

Advances in recombinant protein expression for use in pharmaceutical research

(2013) Rene Assenberg et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Significance of the disulphide bonds of human growth hormone

(2013) Riia K. Junnila et al.   Endokrynologia Polska

The role of human growth hormone's C-terminal disulfide bridge

(2013) R.K. Junnila et al.   GROWTH HORMONE & IGF RESEARCH

Complete Solubilization and Purification of Recombinant Human Growth Hormone Produced in Escherichia coli

(2013) Min-Ji Kim et al.   PLoS One

Facile expression and purification of the antimicrobial peptide histatin 1 with a cleavable self-aggregating tag (cSAT) in Escherichia coli

(2013) Lei Xing et al.   PROTEIN EXPRESSION AND PURIFICATION

Small surfactant-like peptides can drive soluble proteins into active aggregates

(2012) Bihong Zhou et al.   Microbial Cell Factories

Periplasmic production via the pET expression system of soluble, bioactive human growth hormone

(2012) Jonathan T. Sockolosky et al.   PROTEIN EXPRESSION AND PURIFICATION

Streamlined protein expression and purification using cleavable self-aggregating tags

(2011) Lei Xing et al.   Microbial Cell Factories

Self-assembly and gelation properties of α-helix versus β-sheet forming peptides

(2008) A. Saiani et al.   Soft Matter