Results 1 to 10 of about 254,827 (161)

Fusion with heat-resistant obscure (Hero) proteins have the potential to improve the molecular property of recombinant proteins

PLoS ONE, 2022
Although recombinant proteins are widely used in biotechnology and pharmaceutical industries, improving their solubility and stability is often a challenging issue.
Eri Morimoto, Kotaro Tsuboyama, Yukihide Tomari   +2 more
doaj   +4 more sources

Pharmacokinetics of recombinant bifunctional fusion proteins [PDF]

Expert Opinion on Drug Metabolism and Toxicology, 2012
The development of biotechnology has enabled the creation of various recombinant fusion proteins as a new class of biotherapeutics. The uniqueness of fusion proteins lies in their ability to fuse two or more protein domains, providing vast opportunities to generate novel combinations of functions.
Jennica L Zaro, Wei-Chiang Shen
exaly   +3 more sources

Design of an in vivo cleavable disulfide linker in recombinant fusion proteins [PDF]

BioTechniques, 2010
In order to achieve optimal biological activity and desired pharmacokinetic profiles, a dithiocyclopeptide linker was designed for in vivo release of protein domains from a recombinant fusion protein.
Xiaoying Chen, Yun Bai, Jennica L. Zaro, Wei-Chiang Shen   +3 more
doaj   +3 more sources

Application of a novel fusion tag system for enhanced soluble expression of recombinant proteins in Escherichia coli [PDF]

BMC Biotechnology
Background The Escherichia coli expression system is widely used for recombinant protein production, but its utility is often limited by the formation of insoluble inclusion bodies.
Li-Zhen Luo, Jian-Tao Cai, Zi-Ying Tan, Yu-Qing Chen, Zhe Hu, Hai-Hong Wang, Wen-Bin Zhang, Jin-Cheng Ma   +7 more
doaj   +2 more sources

Production of recombinant SARS-COV-2 proteins and diphtheria toxoid CRM197-based fusion [PDF]

The Ukrainian Biochemical Journal, 2021
The quickly emerged global COVID-19 pandemic raised a desperate need in the development of protecting vaccines targeting this disease. Therefore, a generation of effective producers of recombinant SARS-CoV-2 proteins became an urgent task.
O. I. Krynina, S. I. Romaniuk, O. B. Gorbatiuk, O. H. Korchynskyi, А. V. Rebriiev, Ya. S. Kulyk, Ye. O. Kozadaieva, A. A. Siromolot, M. M. Guzyk, D. V. Kolybo, S. V. Komisarenko   +10 more
doaj   +1 more source

The B1 Domain of Streptococcal Protein G Serves as a Multi-Functional Tag for Recombinant Protein Production in Plants

Frontiers in Plant Science, 2022
Plants have long been considered a cost-effective platform for recombinant production. A recently recognized additional advantage includes the low risk of contamination of human pathogens, such as viruses and bacterial endotoxins. Indeed, a great advance
Shi-Jian Song, Hai-Ping Diao, Byeongho Moon, Areum Yun, Inhwan Hwang   +4 more
doaj   +1 more source

Study of native SMAC protein production in the pUbiq expression system: Molecular cloning, biosynthesis and molecular modelling

Electronic Journal of Biotechnology, 2022
Background: In the process of recombinant protein biosynthesis affinity tags are efficient tools to achieve the expected purity and yield during the purification steps.
Pál Salamon, Csongor K. Orbán, Katalin Molnár-Nagy, Zita Kovács, Klára Váncsa, Emese Bálint, Ildikó Miklóssy, Beáta Albert, Gyöngyi Tar, Szabolcs Lányi   +9 more
doaj   +1 more source

Simplified ELISA for Detecting Antibodies to Recombinant Fusion Proteins

BioTechniques, 1997
Sergio Carmona, Wolfgang Prinz, Patrick Arbuthnot   +2 more
doaj   +3 more sources

Refinement of the Fusion Tag PagP for Effective Formation of Inclusion Bodies in Escherichia coli

Microbiology Spectrum, 2023
Methods for efficient insoluble protein production require further exploration. PagP, an Escherichia coli outer membrane protein with high β-sheet content, could function as an efficient fusion partner for inclusion body-targeted expression of ...
Xuefeng Li, Baorong Zhang, Quan Hu, Changchao Chen, Jiahua Huang, Lu Liu, Shengbin Wang   +6 more
doaj   +1 more source

Macromolecular and Solution Properties of the Recombinant Fusion Protein HUG

Biomacromolecules, 2022
The recombinant fusion protein HELP-UnaG (HUG) is a bifunctional product that exhibits human elastin-like polypeptide (HELP)-specific thermal behavior, defined as a reverse phase transition, and UnaG-specific bilirubin-dependent fluorescence emission. HUG provides an interesting model to understand how its two domains influence each other's properties.
Sist, Paola, Bandiera, Antonella, Urbani, Ranieri, Passamonti, Sabina   +3 more
openaire   +4 more sources