The disclosure relates to chromatography ligands, e.g., chromatography ligands comprising at least two binding units and at least one spacer domain, wherein each binding unit comprises one or two immunoglobulin binding domains.

The present invention relates to a chromatography system wherein the chromatography system comprises an eluting system and a capturing system consisting of at least two chromatography units operated alone or in series and a capturing process employing in-line buffer dilution in, which concentrated buffers are blended with water and provided to the chromatography units.

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.

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

A method of producing protein products including alpha-1-proteinase inhibitor, gamma globulin, albumin, and other proteins from plasma includes steps of: (1) adding a salt to the blood product to produce a first intermediate, wherein the salt comprises between 11-13 wt % of the first intermediate; (2) separating the first intermediate to produce a first supernatant and a first paste; (3) adding a salt to the first intermediate to produce a second intermediate, wherein the salt comprises between 21-23 wt % of the second intermediate; (4) separating the second intermediate to produce a second supernatant and a second paste; (5) separating a third intermediate from the second supernatant by affinity chromatography; and (6) separating the third intermediate by ion exchange chromatography to produce an eluate containing the protein product. Advantageously, the inventive methods are simple and produce alpha-1-proteinase inhibitor, gamma globulin, albumin, and other proteins in high yields.

The present disclosure is directed to affinity chromatography devices that include a fibrillated polymer membrane that contains therein inorganic particles that separate a targeted molecule from an aqueous mixture containing the targeted molecule. The targeted molecule includes proteins, antibodies, viral vectors, nucleic acids, and combinations thereof. The inorganic particles may be spherical or irregular in shape. A blend or combination of various sizes and/or shapes of inorganic particles may be utilized. An affinity ligand may be bonded to the inorganic particles and/or to the fibrillated polymer membrane. The affinity chromatography device may be repeatedly used and may be cleaned between uses. In some embodiments, the affinity chromatography devices separate nucleic acids (e.g., mRNA) and viral vectors (e.g., adeno-associated virus) from the aqueous mixture. Manifolds containing multiple affinity chromatography devices in a parallel configuration and multiple manifolds in a parallel configuration are also disclosed.

The present disclosure is directed to affinity chromatography devices that include a fibrillated heat treated polymer membrane that contains therein inorganic particles that separate a targeted molecule from an aqueous mixture containing the targeted molecule. The targeted molecule includes proteins, antibodies, viral vectors, nucleic acids, and combinations thereof. The inorganic particles may be spherical or irregular in shape. A blend or combination of various sizes and/or shapes of inorganic particles may be utilized. An affinity ligand may be bonded to the inorganic particles and/or to the fibrillated polymer membrane. The affinity chromatography device may be repeatedly used and may be cleaned between uses. In some embodiments, the affinity chromatography devices separate nucleic acids (e.g., mRNA) and viral vectors (e.g., adeno-associated virus) from the aqueous mixture. Manifolds containing multiple affinity chromatography devices in a parallel configuration and multiple manifolds in a parallel configuration are also disclosed.

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

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).