A novel protein secretion signal has been developed by combining properties of glycobiology, protein chemistry, and cell biology
Protein expression is a central task to many industries, including biopharmaceutical production, small molecule screening, assay development, biofuel production, agriculture/feed stock preparation and life science research. All of these industries suffer from similar protein quality issues, which relate to misfolding, aggregation, deamidation, poor thermal stability, insolubility, low titer and secretion levels, etc. To address these issues, a novel protein secretion signal has been developed by combining properties of glycobiology, protein chemistry, and cell biology. This signal peptide not only boosts secretion and solubility of proteins that are already secreted, but this powerful N-terminal sequence has been demonstrated to force the secretion of kinases and fluorescent marker proteins – proteins that are known to be located in the cytosolic or transmembrane areas of a cell. Proteins expressed using this new technology are characterized by their increased solubility, improved folding, and increased yields. Purification also requires fewer steps and lower costs, by only purifying the secreted proteins from the cell culture supernatant. At this time, we are applying the technology to enzyme production for cancer treatment development and biofuel production.