High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives

B Jia, CO Jeon - Open biology, 2016 - royalsocietypublishing.org
The ease of genetic manipulation, low cost, rapid growth and number of previous studies
have made Escherichia coli one of the most widely used microorganism species for …

[HTML][HTML] Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system

S Costa, A Almeida, A Castro… - Frontiers in microbiology, 2014 - frontiersin.org
Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is
still the dominant host for recombinant protein production but, as a bacterial cell, it also has …

Proteome-wide identification of ubiquitin interactions using UbIA-MS

X Zhang, AH Smits, GBA Van Tilburg, H Ovaa… - Nature protocols, 2018 - nature.com
Ubiquitin-binding proteins play an important role in eukaryotes by translating differently
linked polyubiquitin chains into proper cellular responses. Current knowledge about …

Rapid online buffer exchange for screening of proteins, protein complexes and cell lysates by native mass spectrometry

ZL VanAernum, F Busch, BJ Jones, M Jia, Z Chen… - Nature protocols, 2020 - nature.com
It is important to assess the identity and purity of proteins and protein complexes during and
after protein purification to ensure that samples are of sufficient quality for further …

[HTML][HTML] Insights on the emerging biotechnology of histidine-rich peptides

H López-Laguna, E Voltà-Durán, E Parladé… - Biotechnology …, 2022 - Elsevier
In the late 70's, the discovery of the restriction enzymes made possible the biological
production of functional proteins by recombinant DNA technologies, a fact that largely …

Spy&Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox

INA Khairil Anuar, A Banerjee, AH Keeble… - Nature …, 2019 - nature.com
Peptide tags are a key resource, introducing minimal change while enabling a consistent
process to purify diverse proteins. However, peptide tags often provide minimal benefit post …

Characterizing metal-binding sites in proteins with X-ray crystallography

KB Handing, E Niedzialkowska, IG Shabalin… - Nature protocols, 2018 - nature.com
Metals have crucial roles in many physiological, pathological, toxicological, pharmaceutical,
and diagnostic processes. Proper handling of metal-containing macromolecule samples for …

Self-cleaving fusion tags for recombinant protein production

Y Li - Biotechnology letters, 2011 - Springer
Fusion expression is a common practice for recombinant protein production. Some fusion
tags confer solubility on the target protein whereas others provide affinity handles that …

Effects of adding poly-histidine tag on stability, antimicrobial activity and safety of recombinant buforin I expressed in periplasmic space of Escherichia coli

S Roshanak, H Yarabbi, F Shahidi… - Scientific Reports, 2023 - nature.com
The lack of cost-effective methods for producing antimicrobial peptides has made it
impossible to use their high potential as a new and powerful class of antimicrobial agents. In …

An insight into fusion technology aiding efficient recombinant protein production for functional proteomics

DK Yadav, N Yadav, S Yadav, S Haque… - Archives of biochemistry …, 2016 - Elsevier
Advancements in peptide fusion technologies to maximize the protein production has taken
a big leap to fulfill the demands of post-genomics era targeting elucidation of …