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.

This tool utilizes orthogonality concepts used for analytical chromatography and apply them to chromatography for downstream processing applications utilizing a small set of product-agnostic, optimally orthogonal resins with which most separations (capture or polishing) can be accomplished. Libraries of components for separation mediums are provided. The library of components is administered to the separation mediums and combination of the separation mediums at varying pHs, and the separability and orthogonality of each is quantified. The separability is a measure of a probability that the separation mediums will separate a pair of components, whereas the orthogonality is a measure of the enhancement in separability upon addition of another separation medium. By identifying those combinations of separation mediums that not only provide advantageous separability, but also high orthogonality, sets of separation mediums can be more easily provided or wholly designed for use in processing applications.

The present invention relates to improved processes and systems for purification of biological molecules, where the processes can be performed in a continuous manner.

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.

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.

The present invention relates to methods for purifying or enriching a biomolecule using multimodal resins and an elution buffer containing a Good's buffer.

The present disclosure provides purification platforms comprising a depth filter step and/or a hydrophobic interaction chromatography (HIC) step. Also disclosed herein are methods of using the purification platforms described herein and compositions obtained therefrom, such as pharmaceutical compositions.

A method of preparing a universal blood product comprising obtaining a blood product; contacting the blood product with (i) hydroxyapatite; (ii) a carbonaceous material comprising at least a mixture of a first carbon particle having macroporous size α and a second carbon particle having macroporous size β; and (iii) at least one support matrix chemically associated with an antigenic determinant.to form a cleansed product; and recovering the cleansed product.

Chromatography resins having mixed mode ligands and methods of using such resins are provided.