A chromatography device is provided comprising a filter housing having an inlet and an outlet and defining a fluid flow path between the inlet and the outlet; a porous filter arranged in the filter housing across the fluid flow path, the filter comprising first porous filter element; and a second porous filter element in contact with the first porous filter element, wherein the first porous filter element comprises at least one anionic exchange (AEX) layer, and the second porous filter element comprises at least one hydrophobic interaction (HIC) layer. A method of purifying nucleic acid using the device is also provided.

The present invention is directed to a method of inactivating virus that is present during production of a polypeptide of interest. In particular, the present invention is directed to a method of on-column virus inactivation using a low pH and high salt wash solution that effectively inactivates viruses with minimum recovery loss of the polypeptide.

The present invention relates to a process for obtaining a potato protein fraction using a specific absorbent. Specifically, the invention relates to the carrier material, which comprises a specific polymeric material, functionalised with suitable ligands. By the use of a functionalised support carrier according to the present invention, a potato protein fraction can be obtained with higher effectiveness.

The present invention relates to a method of purifying peptides and/or polypeptides, said method comprising or consisting of: (a) loading a sample comprising peptides and/or polypeptides under acidic or neutral aqueous conditions on mixed-phase solid phase extraction (SPE) material, wherein said material consists of or comprises reversed phase/ion exchange material; (b) washing said mixed-phase SPE material with (ba) an acidic or neutral composition comprising at least 50% (v/v) organic solvent; and/or (bb) an acidic or neutral aqueous solution; and (c) eluting said peptides and/or polypeptides from said mixed-phase SPE material with an alkaline composition comprising at least 50% (v/v) organic solvent.

The present invention provides a method for reducing the protein aggregation by adjusting the pH below 6.0 of liquid formulation comprising the antibody or fusion protein. The present invention also provides methods for storing the pre-formulation for longer period without using any sugar or additives which can be utilized for preparation of liquid or lyophilized formulation.

The invention relates to parathyroid hormone (PTH) variants and pharmaceutical compositions comprising same. The invention further relates to PTH compositions with improved serum half-life and peak-trough ratios, and methods of controlling serum calcium levels with the PTH variants and compositions of the invention. The invention further relates to methods of treating hypoparathyroidism and/or hypocalcemia due to hypoparathyroidism with the PTH variants and compositions of the invention.

Disclosed herein are methods for the isolation and purification of anti-IL-13 antibodies wherein the use of an affinity chromatographic step results in an antibody composition sufficiently pure for pharmaceutical uses. The methods described herein comprise pH viral reduction/inactivation, ultrafiltration/diafiltration, affinity chromatography (e.g., Protein A affinity chromatography), ion exchange chromatography, and hydrophobic chromatography. Further, the present invention is directed toward pharmaceutical compositions comprising one or more antibodies of the present invention.

Methods of purifying a humanized α4β7 antibody, such as vedolizumab, produced in a mammalian cell culture are described herein, as are compositions resulting from said purification processes.

The present invention relates to a method for purifying a diglycosylated interferon-beta protein and, more specifically, to a method for purifying a diglycosylated interferon-beta protein, wherein a culture solution containing interferon-beta expressed in host cells is obtained, and subjected to affinity chromatography, low-pH inactivation, hydrophobic interaction chromatography, anion-exchange chromatography, and cation-exchange chromatography, and to a diglycosylated interferon-beta protein separated by the method.

Disclosed herein are methods for the isolation and purification of anti-IL-13 antibodies wherein the use of an affinity chromatographic step results in an antibody composition sufficiently pure for pharmaceutical uses. The methods described herein comprise pH viral reduction/inactivation, ultrafiltration/diafiltration, affinity chromatography (e.g., Protein A affinity chromatography), ion exchange chromatography, and hydrophobic chromatography. Further, the present invention is directed toward pharmaceutical compositions comprising one or more antibodies of the present invention.