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Saccharomyces cerevisiae was used as the host for expression of fusion protein PA-1-linker-HGFI (pH) and his-tag purification was used to purify recombinant protein pH.
In 1981 for the first time the expression of recombinant proteins in S. cerevisiae was described but its applications as a host for expression of heterologous proteins in this yeast has diminished due to some limitations.
In this proof of concept work, we demonstrate that the cyanobacterium Synechocystis sp. PCC 6803 is an eminent heterologous host for expression of metabolically engineered cytochrome P450-dependent pathways exemplified by the dhurrin pathway from Sorghum bicolor comprising two membrane bound cytochromes P450s (CYP79andand CYP71E1) and a soluble glycosyltransferase (UGT85B1).
E. coli BL21 (DE3) was used as the host for expression of recombinant protein.
E. coli BL21 (DE3) strain (Novagen) was used as the host for expression of recombinant proteins.
These observations, therefore, indicate presence of suitable co-operativity between the virus and the host for expression of viral oncogenes.
Similar(39)
Similar results were obtained using E. coli C41 (DE3) and E. coli C43 (DE3) as hosts for expression.
B. subtilis 168 (trpC2) and E. coli DH5α respectively used as hosts for expression of plasmid-encoded phytase and molecular cloning were generously gifted by Dr. Emmanuelle Maguin.
Yeasts, especially S. cerevisiae, are increasingly being used as hosts for expression of protein biocatalysts and multi-enzyme pathways for the synthesis of fine chemicals and small molecular weight compounds of medicinal and nutritional importance.
Escherichia coli strains JM109 and DH5α served as hosts for expression vectors and recombinant plasmids.
Among these microorganisms, Escherichia coli is one of the most frequently used hosts for expression of recombinant genes.
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