The present invention is within the field of chromatography. More precisely, it relates to a novel chromatography medium, namely a hydrophobic medium provided with different lids excluding molecules over a certain size due to the porosity of the hydrophobic medium and/or the porosity of the lid. The invention also relates to use of the separation medium for purification of large molecules, which do not enter the separation medium, as well as small molecules, which enter the separation medium and are eluted from there.

The present invention relates to a method for purifying an enveloped virus. The present invention further relates to an enveloped virus or a plurality of enveloped viruses obtainable by said method.

Provided herein are methods of separating host cell lipases from a production protein in chromatographic processes and methods of improving polysorbate-80 stability in a production protein formulation by separating host cell lipases from the production protein using chromatographic processes. Also provided are pharmaceutical compositions comprising less than 1 ppm of a host cell lipase.

Adsorptive media for chromatography, particularly ion-exchange chromatography, derived from a shaped fiber. In certain embodiments, the functionalized shaped fiber presents a fibrillated or ridged structure which greatly increases the surface area of the fibers when compared to ordinary fibers. Also disclosed herein is a method to add surface pendant functional groups that provides cation-exchange or anion-exchange functionality to the high surface area fibers. This pendant functionality is useful for the ion-exchange chromatographic purification of biomolecules, such as monoclonal antibodies (mAbs).

In certain embodiments, the present invention provides a method of measuring the level of hydrophobicity of a chromatographic resin. In certain embodiments, the present invention provides a method of selecting a chromatographic resin condition for purifying a protein of interest from a mixture, wherein the protein of interest has low or no aggregation formation during chromatography. In certain embodiments, the present invention provides a method of selecting a chromatographic resin from a plurality of chromatographic resins for purifying a protein of interest from a mixture, wherein the protein of interest has low or no aggregation formation during chromatography.

Provided are a platelet-derived growth factor B derivative, the encoding nucleic acid molecule thereof, and a vector and host cell having the nucleic acid molecule. Also provided are a preparation method for the mutant, and the use of the mutant in preparing medications for promoting cell division, cell proliferation, wound healing, skin regeneration, bone and tooth defect regeneration, and joint repair.

The invention is directed to methods for purifying recombinant proteins, e.g. HIV-1 envelope trimers and/or nanoparticles, wherein the methods do not use an affinity step.

Methods for extracting one or more chemical compounds from cannabis plant material are provided. In some embodiments, the method may comprise: providing the cannabis plant material; extracting the cannabis plant material with a solvent to produce a solvent extract; and filtering the solvent extract through a filter material to produce a filtered extract. Also provided are related systems. Related cannabis extracts and products comprising cannabis extracts are also provided.

The present invention relates to method of purifying charge-shielded proteins from a cell lysate or periplasmic releasate using hydrophobic interaction chromatography as a first chromatography steps. Also provided herein are compositions comprising charge-shielded proteins and methods of treatment using purified charge-shielded proteins.

Provided is a complex composition, of which positional isomers are minimized by using a N-terminus of an immunoglobulin Fc region as a binding site when the immunoglobulin Fc region is used as a carrier. Also provided are a protein complex which is prepared by N-terminal-specific binding of immunoglobulin Fc region, thereby prolonging blood half-life of the physiologically active polypeptide, maintaining in vivo potency at a high level, and having no risk of immune responses, a preparation method thereof, and a pharmaceutical composition including the same for improving in vivo duration and stability of the physiologically active polypeptide. The protein complex may be usefully applied to the development of long-acting formulations of various physiologically active polypeptide drugs.