Abstract:
In a method for facilitating selection of chromatography parameters for manufacturing a therapeutic protein, one or more process parameter values associated with a hypothetical chromatography process, and one or more molecular descriptors descriptive of the therapeutic protein, are received. The method also includes predicting a performance indicator for the hypothetical chromatography process at least by analyzing the one or more process parameters and the one or more molecular descriptors using a machine learning model. The machine learning model is a regression tree model, an extreme gradient boost model, or an elastic net model. The method also includes causing the predicted performance indicator, and/or an indication of whether the predicted performance indicator satisfies one or more acceptability criteria, to be presented to a user via a user interface.
Abstract:
A method of refolding proteins expressed in non-mammalian cells present in concentrations of 2.0 g/L or higher is disclosed. The method comprises identifying the thiol pair ratio and the redox buffer strength to achieve conditions under which efficient folding at concentrations of 2.0 g/L or higher is achieved and can be employed over a range of volumes, including commercial scale.
Abstract:
Methods of purifying proteins expressed in non-mammalian expression systems in a non-native soluble form directly from cell lysate are disclosed. Methods of purifying proteins expressed in non-mammalian expression systems in a non-native limited solubility form directly from a refold solution are also disclosed. Resin regeneration methods are also provided.
Abstract:
Methods of inactivation of a virus in a sample comprising a protein component are provided. Also provided are methods of reducing protein degradation or modification in to the presence of a reactive species, such as a reactive species generated as a result of UV exposure, are also provided. In another aspect, a method of reducing oxidation of methionine residues, tryptophan residues or both methionine and tryptophan residues in a protein subjected to UV light is provided. The disclosed methods can be performed at any scale and can be automated as desired.
Abstract:
A method of refolding proteins expressed in non-mammalian cells present in concentrations of 2.0 g/L or higher is disclosed. The method comprises identifying the thiol pair ratio and the redox buffer strength to achieve conditions under which efficient folding at concentrations of 2.0 g/L or higher is achieved and can be employed over a range of volumes, including commercial scale.
Abstract:
Methods of determining the dose of UVC light delivered to a sample comprising a low optical transmission complex fluid are provided. Also provided are methods of inactivation of an organism, such as a spore, a bacteria or a virus, in a sample comprising dose of UVC light delivered to a sample comprising a low optical transmission complex fluid.
Abstract:
Methods of determining the dose of UVC light delivered to a sample comprising a low optical transmission complex fluid are provided. Also provided are methods of inactivation of an organism, such as a spore, a bacteria or a virus, in a sample comprising dose of UVC light delivered to a sample comprising a low optical transmission complex fluid.
Abstract:
Methods of purifying proteins expressed in non-mammalian expression systems in a non-native soluble form directly from cell lysate are disclosed. Methods of purifying proteins expressed in non-mammalian expression systems in a non-native limited solubility form directly from a refold solution are also disclosed. Resin regeneration methods are also provided.
Abstract:
Methods of purifying proteins expressed in non-mammalian expression systems in a non-native soluble form directly from cell lysate are disclosed. Methods of purifying proteins expressed in non-mammalian expression systems in a non-native limited solubility form directly from a refold solution are also disclosed. Resin regeneration methods are also provided.