Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Jorge M Montfort-Gardeazabal"'
Autor:
Megan M. McEvoy, Xristo Zarate, Bryan D. Santos, Jéssica J. Gómez-Lugo, Jorge M Montfort-Gardeazabal, David A. Perez-Perez
Publikováno v:
Methods in Molecular Biology ISBN: 9781071607749
The bacterium Escherichia coli is still considered the first option as a microbial cell factory for recombinant protein production, and affinity chromatography is by far the preferred technique for initial purification after protein expression and ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::637d85d4d9bd8f8762f5c4826221b561
https://doi.org/10.1007/978-1-0716-0775-6_22
https://doi.org/10.1007/978-1-0716-0775-6_22
Autor:
Jessica J, Gomez-Lugo, Bryan D, Santos, David A, Perez-Perez, Jorge M, Montfort-Gardeazabal, Megan M, McEvoy, Xristo, Zarate
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2178
The bacterium Escherichia coli is still considered the first option as a microbial cell factory for recombinant protein production, and affinity chromatography is by far the preferred technique for initial purification after protein expression and ce
Autor:
Jorge M, Montfort-Gardeazabal, Pilar C Morales-San, Claudio, Nestor G, Casillas-Vega, Xristo, Zarate
Publikováno v:
Protein and peptide letters. 28(1)
The heterologous production of antimicrobial peptides in bacterial models can produce insoluble proteins due to the lack of proper folding. Fusion proteins have been used to increase the expression and solubility of these types of proteins with varyi
Publikováno v:
Protein Expression and Purification. 178:105784
We have previously shown that the small metal-binding proteins CusF3H+ and SmbP can be used as fusion proteins for the expression and purification of recombinant proteins in Escherichia coli. Because of their small size, both around 10 kDa, they are