A method exosome purification and characterization is contemplated, comprising the steps of secondary two-stage tangential ultrafiltration to produce an extracted solution, pretreatment of the extracted solution for characterization, characterization of the extracted solution to detect particle size and concentration, and freeze-drying of the extracted solution. An exosome purification integrated device is also contemplated. Through the disclosed methods and devices, exosomes may be better purified and characterized in a manner that results in high practical value to overcome the problems associated with conventional exosome purification processes on the market today, including tedious purification processes, long durations, and high costs.

A method exosome purification and characterization is contemplated, comprising the steps of secondary two-stage tangential ultrafiltration to produce an extracted solution, pretreatment of the extracted solution for characterization, characterization of the extracted solution to detect particle size and concentration, and freeze-drying of the extracted solution. An exosome purification integrated device is also contemplated. Through the disclosed methods and devices, exosomes may be better purified and characterized in a manner that results in high practical value to overcome the problems associated with conventional exosome purification processes on the market today, including tedious purification processes, long durations, and high costs.

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.

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.

The present disclosure pertains to compositions comprising anti-VEGF proteins and methods for producing such compositions.

The present disclosure pertains to compositions comprising anti-VEGF proteins and methods for producing such compositions.

The present invention relates to a method for preparing a TNFR-Fc fusion protein mixture comprising a target content of hydrophobic chromatogram peak 3, and to a method for adjusting a content of hydrophobic chromatogram peak 3. Specifically, the present invention relates to (a) a method for preparing a TNFR-Fc fusion protein mixture using a hydrophobic interaction chromatograph medium containing an aromatic functional group, which is pre-equilibrated with an equilibration buffer comprising sodium chloride or ammonium sulfate, and a sample comprising a TNFR-Fc fusion protein mixture liquid produced from mammalian cells, and to a method for adjusting the content of hydrophobic chromatogram peak 3 by hydrophobic chromatography using an equilibration buffer containing a predetermined concentration of sodium chloride or ammonium sulfate.

The present invention relates to a method for preparing a TNFR-Fc fusion protein mixture comprising a target content of hydrophobic chromatogram peak 3, and to a method for adjusting a content of hydrophobic chromatogram peak 3. Specifically, the present invention relates to (a) a method for preparing a TNFR-Fc fusion protein mixture using a hydrophobic interaction chromatograph medium containing an aromatic functional group, which is pre-equilibrated with an equilibration buffer comprising sodium chloride or ammonium sulfate, and a sample comprising a TNFR-Fc fusion protein mixture liquid produced from mammalian cells, and to a method for adjusting the content of hydrophobic chromatogram peak 3 by hydrophobic chromatography using an equilibration buffer containing a predetermined concentration of sodium chloride or ammonium sulfate.

The present invention provides a separation material that comprises porous polymer particles comprising a styrene-based monomer as a monomer unit; and a coating layer comprising a macromolecule having hydroxyl groups, which covers at least a portion of the surface of the porous polymer particles, and the separation material has a 5% compressive deformation modulus of 100 to 1,000 MPa, and has a mode diameter in the pore size distribution of 0.1 to 0.5 μm.

The present invention relates to dimers comprising a first polypeptide and a second polypeptide, wherein each of said first and second polypeptide comprises at least one immunoglobulin single variable domain (1ISVD) and a C-terminal extension comprising a cysteine moiety (preferably at the C-terminus), wherein said first polypeptide and said second polypeptide are covalently linked via a disulfide bond between the cysteine moiety of said first polypeptide and the cysteine moiety of said second polypeptide, in which the dimer outperformed the benchmark constructs, e.g. cognate multivalent and multispecific constructs, in various assays. The present invention provides methods for making the dimers of the invention.