Cargando…
Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive Escherichia coli protein, RpoS
BACKGROUND: The most efficient method for enhancing solubility of recombinant proteins appears to use the fusion expression partners. Although commercial fusion partners including maltose binding protein and glutathione-S-transferase have shown good performance in enhancing the solubility, they cann...
Autores principales: | Park, Jin-Seung, Han, Kyung-Yeon, Lee, Jong-Ho, Song, Jong-Am, Ahn, Keum-Young, Seo, Hyuk-Seong, Sim, Sang-Jun Jun, Kim, Seung-Wook, Lee, Jeewon |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2278137/ https://www.ncbi.nlm.nih.gov/pubmed/18282304 http://dx.doi.org/10.1186/1472-6750-8-15 |
Ejemplares similares
-
Polymorphism and selection of rpoS in pathogenic Escherichia coli
por: Dong, Tao, et al.
Publicado: (2009) -
RpoS role in virulence and fitness in enteropathogenic Escherichia coli
por: Mata, Gardênia Márcia Silva Campos, et al.
Publicado: (2017) -
Function, Evolution, and Composition of the RpoS Regulon in Escherichia coli
por: Schellhorn, Herb E.
Publicado: (2020) -
Conversion of RpoS(−) Attenuated Salmonella enterica Serovar Typhi Vaccine Strains to RpoS(+) Improves Their Resistance to Host Defense Barriers
por: Burda, Whittney N., et al.
Publicado: (2018) -
Chitobiose utilization in Borrelia burgdorferi is dually regulated by RpoD and RpoS
por: Rhodes, Ryan G, et al.
Publicado: (2009)