Thomas S. Vedvick

TL;DR: The Pichia pastoris heterologous gene expression system has been utilized to produce attractive levels of a variety of intracellular and extracellular proteins of interest and improvements in understanding and application have improved its utility even further.

TL;DR: Affinity-purified, polyclonal antibodies to the gamma subunit of the dihydropyridine (DHP)-sensitive, voltage-dependent calcium channel have been used to isolate complementary DNAs to the rabbit skeletal muscle protein from an expression library, and the deduced primary structure indicates that it is a glycosylated hydrophobic protein.

TL;DR: A synthetic gene encoding aprotinin (bovine pancreatic trypsin, inhibitor) was fused to the Saccharomyces cerevisiae prepro alpha mating factor leader sequence at the dibasic amino acid processing site, leading to the secretion of a biologically active aProtinin containing only a Glu-Ala N-terminal extension.

TL;DR: The use of the methylotrophic industrial yeast Pichia pastoris as a host system for the large scale production of the KPI domain of PN-2AβPP, a secreted isoform of the Alzheimer's amyloid β-protein precursor that contains the Kunitz-type protease inhibitor (KPI) domain, is described.

TL;DR: Improvements in strains have boosted the yield of proteins and peptides to the commercially feasible range and the Pichia pastoris expression system will soon be used to manufacture proteins for human clinical trials.