The invention discloses a separation matrix comprising a plurality of multimodal ligands covalently coupled to a support, wherein said support is a membrane comprising nonwoven polymer fibers and wherein said ligands are capable of interacting with a target biomacromolecule. Further, the invention discloses separation methods using the separation matrix.

The invention discloses a separation matrix comprising a plurality of multimodal ligands covalently coupled to a support, wherein said support is a membrane comprising nonwoven polymer fibers and wherein said ligands are capable of interacting with a target biomacromolecule. Further, the invention discloses separation methods using the separation matrix.

The present disclosure relates generally to the manufacturing of gene therapy products, and specifically to methods of purifying an enveloped virus from a cell culture fluid, comprising an endonuclease and/or anion exchange chromatography.

The present invention describes a simple purification process for recombinant human serum albumin. The process results in highly purified protein with limited number of purification steps. The broth containing human albumin is clarified by centrifugation and microfiltration, diafiltered and captured by cation exchange chromatography by a process that allows 140-230 mg of albumin to be captured per mi of resin. Product related impurities are removed by hydrophobic interaction chromatography, optimised to allow 87-97% recovery in flow through mode. The final series of processes are so combined that there is easy transition from one step to the next with minimal interventions and adjustments. The entire process of purification is completed within two days from harvest to final product. Thus a cost-effective process with improved recovery of protein at each step is developed. The purified human serum albumin is analyzed for purity and shows physicochemical characteristics that are similar to standard albumin.

The present invention relates to a method for removing host cell DNA from a sample comprising infectious viral particles and host cell DNA by anion exchange chromatography in the presence of at least one of a non-ionic surfactant, a sugar and a protein and to a method for purifying recombinant infectious viral particles from a host cell culture employing such an anion exchange chromatography step.

Provided herein are methods and compositions for the separation of an adeno-associated virus (AAV) particle from a mixture of the AAV and at least one contaminant using anion exchange chromatography. These methods and compositions allow for improved purification of complete AAV particles from contaminants such as AAV particles that lack a complete genome (e.g., empty capsids) and AAV degradation products.

The disclosure provides methods for the isolation, separation, and purification of antibodies. The method comprises an affinity chromatography capture step, anion exchange chromatography polishing step, and cation exchange chromatography polishing step.

The disclosure provides methods for the isolation, separation, and purification of antibodies. The method comprises an affinity chromatography capture step, anion exchange chromatography polishing step, and cation exchange chromatography polishing step.

The invention relates to a process for enriching IgA (and IgM) from IgA-comprising material. In particular, it relates to a sequential elution process of an anion exchanger that leads to an advantageous enrichment and separation of monomeric and dimeric IgA.

Compounds are provided for the capture of polycyclic aromatic hydrocarbons. The compound is selected from formula (I) and formula (II): ##STR00001##
The compound includes a salt formed with a suitable counter anion.