Results 1 to 10 of about 282,766 (336)

Simplified ELISA for Detecting Antibodies to Recombinant Fusion Proteins

BioTechniques, 1997
Sergio Carmona, Wolfgang Prinz, Patrick Arbuthnot   +2 more
doaj   +5 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   +4 more sources

Turn TRAIL Into Better Anticancer Therapeutic Through TRAIL Fusion Proteins [PDF]

Cancer Medicine
Background TNF‐related apoptosis‐inducing ligand (TRAIL) belongs to the tumor necrosis factor superfamily. TRAIL selectively induces apoptosis in tumor cells while sparing normal cells, which makes it an attractive candidate for cancer therapy ...
Yan Wang, Xin Qian, Yubo Wang, Caiyuan Yu, Li Feng, Xiaoyan Zheng, Yaya Wang, Qiuhong Gong   +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

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   +2 more sources

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

Pharmacokinetics of recombinant bifunctional fusion proteins [PDF]

Expert Opinion on Drug Metabolism & 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.
Xiaoying Chen, Jennica L. Zaro, Wei-Chiang Shen   +2 more
openaire   +3 more sources

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

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

Osteoinductive recombinant silk fusion proteins for bone regeneration [PDF]

Acta Biomaterialia, 2017
Protein polymers provide a unique opportunity for tunable designs of material systems due to the genetic basis of sequence control. To address the challenge of biomineralization interfaces with protein based materials, we genetically engineered spider silks to design organic-inorganic hybrid systems.
Dinjaski, N, Plowright, R, Zhou, S, Belton, DJ, Perry, CC, Kaplan, DL   +5 more
openaire   +4 more sources