A method for removal of host cell DNA from a sample containing a species of desired protein, virus, or extracellular vesicle comprising the steps of: Loading a substrate bearing an anionic metal affinity ligand with a metal ion, Equilibrating the substrate with a buffer having a pH in the range of pH 6 to pH 10, and a salt concentration in a concentration range up to 1 M which salt is not forming a chemical complex with the anionic metal affinity ligand, Contacting the sample with the metal-loaded anionic metal affinity substrate, Separating the substrate from the sample, wherein the sample has reduced content of contaminating DNA.

A solid-phase chelator material usable for the purification of proteins. The solid-phase chelator material comprises a solid phase, polyamine groups bound to the solid phase and chelating groups bound to the polyamine groups. At least a part of the polyamine groups is connected with at least two chelating groups per polyamine group. Each chelating group comprises one or several aminopolycarboxylic acid groups (APA groups), with the proviso that the number of APA groups per polyamine group connected with at least two cheating groups is at least three.

Chromatography media and devices containing chromatography media are disclosed. Methods of making chromatography devices and methods of using chromatography devices containing the chromatography media are also disclosed.

In some embodiments, the present disclosure pertains to a method for capturing alkenes that includes: associating the alkenes with metal-organic frameworks, where the metal-organic frameworks includes one or more metals and one or more ligands coordinated with the one or more metals, and where the metal-organic frameworks are conductive; and oxidizing the metal-organic frameworks, where the oxidizing results in a capturing of the alkenes by the metal-organic frameworks. Additional embodiments of the present disclosure pertain to a system for capturing alkenes that includes: metal-organic frameworks, where the metal-organic frameworks include one or more metals and one or more ligands coordinated with the one or more metals, and where the metal-organic frameworks are conductive; and an alkene feed source associated with the metal-organic frameworks, where the alkene feed source is configured to deliver an alkene feed to the system.

A method for separating full Adeno-associated virus (AAV) capsids from empty AAV capsids in a buffered mixture comprising full AAV capsids, empty AAV capsids, comprising the steps of contacting the buffered mixture with a first substrate bearing a metal affinity ligand attached to the first substrate, said metal affinity ligand having the ability to complex metal ions via three or more nitrogen atoms, separating empty AAV capsids from full AAV capsids by eluting with a pH gradient, a salt gradient, a metal ion gradient or a combination thereof in the presence of multivalent cations bound to the metal affinity ligand to obtain a purified full AAV capsid fraction.

For removing contaminating DNA in the mixture or purified AAV capsid fraction, the method of the invention can be combined with contacting of the buffered mixture or the purified full AAV capsid fraction with a second substrate bearing a metal affinity ligand attached to the second substrate in the presence of multivalent cations bound to the metal affinity ligand, said metal affinity ligand comprises two or more negatively charged carboxylic acid residues.

The present disclosure provides surface functionalized affinity membranes. The surface functionalized affinity membranes can provide increased binding capacity through improved coupling chemistries, ligand densities, spacer arm types, and spacer arm lengths. Methods of preparing the surface functionalized affinity membranes and methods of using the surface functionalized affinity membranes to isolate targets of interest, including nucleic acid molecules and proteins, from a sample are also provided.

The invention relates to the isolation or extraction of exosomes.

Disclosed here are compositions comprising recombinant acid sphingomyelinase (rASM) having desired purity, specific activity, and/or rASM isoforms. Also provided are methods for making and purifying such compositions, comprising chromatography steps. Further provided are methods of modulating rASM specific activity in a composition, and methods of modulating rASM isoforms in a composition. The methods disclosed here can be particularly useful for manufacturing pharmaceutical compositions comprising rASM for treating acid sphingomyelinase deficiency (ASMD).

A method for transferring a radioisotope which is fixed on a first stationary phase contained in a first chromatography column to a second stationary phase contained in a second chromatography column, to fix the radioisotope on the second stationary phase, wherein the radioisotope is selected from the radioactive isotopes of thorium, radium, lead, bismuth and uranium, the method comprising at least the following steps: a) eluting the radioisotope from the first stationary phase with an aqueous solution A1 comprising a citric acid salt as an agent complexing the radioisotope, whereby an aqueous solution A2 which comprises citrate complexes of the radioisotope is obtained; b) dissociating the citrate complexes of the radioisotope present in the aqueous solution A2 by modifying the pH of the aqueous solution A2, whereby an aqueous solution A3 comprising the decomplexed radioisotope is obtained; c) loading the second stationary phase with the aqueous solution A3; and d) washing at least one the second stationary phase with an aqueous solution A4.

The present invention relates to a novel chromatography media, more closely a novel IMAC (Immobilized Metal Affinity Chromatography) media. The novel chromatography media comprises a pentaligand and provides high dynamic binding capacity as well as high purity of the sample proteins purified on the media of the invention.