The Escherichia coli expression system is a cornerstone in recombinant protein production, favored for its well-characterized metabolic pathways, rapid cell growth, high protein expression levels, and clear genetic background. Despite these advantages, a significant challenge in using this system is the propensity for protein aggregation into inclusion bodies.
Mammalian protein expression systems are now widely used in the biopharmaceutical industry for producing complex recombinant proteins. These systems use mammalian cell lines like Chinese hamster ovary (CHO) cells and human embryonic kidney (HEK) 293 cells.
Pichia pastoris, a methylotrophic yeast, has emerged as a highly efficient and widely used eukaryotic host for the production of recombinant proteins. This system combines the advantages of eukaryotic post-translational modifications with the rapid growth and scalability of yeast-based expression systems, making it particularly suitable for the production of complex proteins that require glycosylation and other modifications for proper folding and functionality.
Escherichia coli (E. coli) is one of the most widely used prokaryotic expression systems for the production of recombinant proteins. Its popularity stems from several key advantages, including ease of genetic manipulation, rapid growth rate, and cost-effectiveness. E. coli has been extensively studied and optimized for protein expression, making it a cornerstone in both research and industrial applications.
Protein expression is a critical biological process that involves the synthesis, folding, localization, and regulation of proteins in response to the functional demands of the body. It represents the dynamic output of the genome, where specific proteins are produced to meet cellular and physiological needs
