Abstract: A traffic safety sign assembly for guiding traffic around a vehicle parked on a shoulder of a roadway includes a sign that is positionable on a vehicle that is parked on a shoulder of a roadway. In this way the sign is visible to oncoming traffic on the roadway. Arrow indicia are printed on the sign to direct oncoming traffic away from the vehicle. A plurality of sign light emitters is each integrated into the sign to emit light outwardly from the sign. In this way the sign light emitters enhance visibility of the sign for the oncoming traffic. The plurality of sign light emitters is strategically arranged on the sign to indicate a preferred direction of travel. In this way the sign light emitters visually communicate the preferred direction of travel to the oncoming traffic.

Abstract: A traffic safety sign assembly for guiding traffic around a vehicle parked on a shoulder of a roadway includes a sign that is positionable on a vehicle that is parked on a shoulder of a roadway. In this way the sign is visible to oncoming traffic on the roadway. Arrow indicia are printed on the sign to direct oncoming traffic away from the vehicle. A plurality of sign light emitters is each integrated into the sign to emit light outwardly from the sign. In this way the sign light emitters enhance visibility of the sign for the oncoming traffic. The plurality of sign light emitters is strategically arranged on the sign to indicate a preferred direction of travel. In this way the sign light emitters visually communicate the preferred direction of travel to the oncoming traffic.

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: 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.

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 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: 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: 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: 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: 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 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: 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 butler 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: 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 foe 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: 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.