The K. lactis Protein Expression Kit provides a simple method for cloning and expressing genes of interest in the yeast Kluveromyces lactis. This system offers rapid high cell density growth, access to protein folding and glycosylation machinery, and expression of genes that are toxic to E. coli. The methanol containing medium and antibiotic requirements of Pichia pastoris are eliminated. With protocols and highly competent K. lactis cells included, this system can take you from bench top to large scale production with ease.

Secreted protein processing in K. lactis. In the nucleus, an integrated expression vector encoding a fusion between the ?-MF domain (blue) and a desired protein (black) is expressed. A signal peptide in the ?-MF domain directs entry of the fusion protein into the endoplasmic reticulum (ER) and is removed by signal peptidase (SP). The fusion protein is transported to the Golgi where the Kex protease removes the ?-MF domain. The protein of interest is then secreted from the cell.