Non-repressing carbon sources for alcohol oxidase (AOX1) promoter of Pichia pastoris.

Non-Repressing Carbon Sources for Alcohol Oxidase (AOXI) Promoter of Pichia pastoris

A novel methanol-free Pichia pastoris system for recombinant protein expression

BACKGROUND As one of the most popular expression systems, recombinant protein expression in Pichia pastoris relies on the AOX1 promoter (P AOX1 ) which is strongly induced by methanol. However, the toxic and inflammatory nature of methanol restricts its application, especially in edible and medical products. Therefore, constructing a novel methanol-free system becomes necessary. The kinases inv...

Production of Recombinant Human Granulocyte-Colony Stimulating Factor by Pichia pastoris

Human granulocyte-colony stimulating factor (hG-CSF) cDNA was expressed in the methylotrophic yeast Pichia pastoris under the control of the alcohol oxidase (AOX1) promoter. An expression vector for hG-CSF secretion was constructed using vector pPIC9. Higher levels of hG-CSF was obtained using a P. pastoris Mut+ (methanol utilization fast) phenotype. The effects of environmental factors such as...

An upstream activation sequence controls the expression of AOX1 gene in Pichia pastoris.

Alcohol oxidase I gene (AOX1) promoter (P(AOX1)) is a key promoter in the methylotrophic yeast Pichia pastoris. To identify the cis-acting element in the AOX1 promoter, we constructed expression plasmids in which the green fluorescent protein (GFP) gene coding region was fused to a series of internal deletion mutants of the AOX1 promoter. By analyzing the expression and transcription level of G...

Evaluation of pH/buffering conditions effect on the optimization of Recombinant Human Erythropoietin expression in the methylotrophic yeast, Pichia pastoris

Expression of recombinant proteins and drugs in Pichia pastoris has been in development since the late 1980s and the number of recombinant proteins produced in P. pastoris has increased significantly in the past several years. Unlike bacteria, this strain is capable of producing complex proteins with post translational modifications such as correct folding, glycosylation, proteolytic maturation...