Results 1 to 10 of about 391,068 (308)

TLR5-dependent immunogenicity of a recombinant fusion protein containing an immunodominant epitope of malarial circumsporozoite protein and the FliC flagellin of Salmonella Typhimurium [PDF]

open access: yesMemorias do Instituto Oswaldo Cruz, 2011
Recently, we described the improved immunogenicity of new malaria vaccine candidates based on the expression of fusion proteins containing immunodominant epitopes of merozoites and Salmonella enterica serovar Typhimurium flagellin (FliC) protein as an ...
Ariane Guglielmi Ariza Camacho   +7 more
doaj   +6 more sources

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

open access: yesBMC 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   +7 more
doaj   +2 more sources

A standardized set of pNX vectors for enhanced soluble expression of recombinant proteins in E. coli using small fusion tags [PDF]

open access: yesMicrobial Cell Factories
Background The production of recombinant proteins in Escherichia coli (E. coli) is often hampered by the formation of inclusion bodies. While fusion tags can enhance solubility, existing systems are hampered by a lack of standardization, with tags ...
Li-Zhen Luo   +5 more
doaj   +2 more sources

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

open access: yesThe 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   +10 more
doaj   +1 more source

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

open access: yesPLoS 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   +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

open access: yesFrontiers 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   +4 more
doaj   +1 more source

Pharmacokinetics of recombinant bifunctional fusion proteins [PDF]

open access: yesExpert 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   +2 more
openaire   +2 more sources

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

open access: yesElectronic 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   +9 more
doaj   +1 more source

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

open access: yesMicrobiology 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   +6 more
doaj   +1 more source

Osteoinductive recombinant silk fusion proteins for bone regeneration [PDF]

open access: yesActa 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   +5 more
openaire   +3 more sources

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