Cargando…
Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
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 its issues: the aggregation of foreign proteins into insoluble inclusion bodies is perhaps the main limiting...
Autores principales: | Costa, Sofia, Almeida, André, Castro, António, Domingues, Lucília |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928792/ https://www.ncbi.nlm.nih.gov/pubmed/24600443 http://dx.doi.org/10.3389/fmicb.2014.00063 |
Ejemplares similares
-
A novel adjuvant-free H fusion system for the production of recombinant immunogens in Escherichia coli: Its application to a 12 kDa antigen from Cryptosporidium parvum
por: Costa, Sofia J, et al.
Publicado: (2013) -
Fusion Tag Design Influences Soluble Recombinant Protein Production in Escherichia coli
por: Köppl, Christoph, et al.
Publicado: (2022) -
Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli
por: Brewer, M Kathryn, et al.
Publicado: (2014) -
Tag-mediated single-step purification and immobilization of recombinant proteins toward protein-engineered advanced materials
por: Freitas, Ana I., et al.
Publicado: (2021) -
Cloning, Expression, and Purification of Histidine-Tagged Escherichia coli Dihydrodipicolinate Reductase
por: Trigoso, Yvonne D., et al.
Publicado: (2016)