Provided herein are methods of separating host cell lipases from an anti-LAG3 antibody or antigen binding fragment in chromatographic processes and methods of improving polysorbate-80 stability in an anti-LAG3 antibody formulation by separating host cell lipases from the anti-LAG3 antibody or antigen binding fragment using chromatographic processes. Also provided are pharmaceutical compositions comprising an anti-LAG3 antibody or antigen binding fragment and less than 2 ppm of a host cell lipase.

Provided herein are methods of preparing EVs, e.g., exosomes, associated with or encapsulated various cyclic dinucleotides, including STING agonists. Also provided herein are methods of loading EVs, e.g., exosomes, with various cyclic dinucleotides, including STING agonists.

A process for the purification of an aqueous hydrogen peroxide solution includes the following steps: (a) the treatment of an aqueous hydrogen peroxide solution with at least one first reverse osmosis system, (b) the treatment of the obtained hydrogen peroxide solution with at least one first stabilizer, (c) the treatment of the obtained hydrogen peroxide solution with at least one purification mean selected from adsorption resins, ion exchange resins, and combinations thereof.

An aqueous hydrogen peroxide solution obtainable thereby is described. The use of the aqueous hydrogen peroxide solution in the manufacture of microelectronic components and semiconductors is also described.

A system for separating competing anions from per- and polyfluoroalkyl substances (PFAS) in a flow of water contaminated with PFAS and elevated levels of competing anions that includes a separation subsystem which receives the flow of water contaminated with PFAS and elevated levels of competing anions and separates competing anions from the PFAS and concentrates the PFAS to produce a treated flow of water having separated competing anions therein and a flow of water having a majority of PFAS therein. At least one anion exchange vessel having an anion exchange resin therein receives the flow of water having a majority of PFAS therein and removes PFAS from the water to produce a flow of treated water having a majority of the PFAS removed. The separation of competing anions by the separation subsystem increases the treatment capacity of the anion exchange resin to remove PFAS from the contaminated water.

A filter cartridge assembly for an ice making appliance having a rectilinear filter cartridge with a plurality of partitions that are positioned within an internal chamber, form multiple sub-chambers, and create a non-linear pathway for the flow of water through the filter cartridge. Filter media positioned in the sub-chambers of the filter cartridge are configured to remove dissolved solids from water travelling through the filter cartridge and used by the appliance to create ice, including clear ice.

A method for removing coloration from a drug substance solution of protein preparation, in particular, antibody preparation, a method for preparing drug substance solution of protein preparations including it, as a part thereof, and highly concentrated, colorless drug substance solutions thereof are disclosed. The method removes terminal glycation products causing the coloration in the drug substance solution of protein preparation, in particular, antibody preparation, by anion-exchange chromatography, making it possible to provide colorless drug substance solutions.

The disclosure discloses a genetically engineered strain for producing porcine myoglobin and fermentation and purification thereof, and belongs to the technical field of genetic engineering. The disclosure realizes efficient secretion and expression of porcine myoglobin by integrating the gene of porcine myoglobin in P. pastoris. On this basis, optimization of the medium and culture conditions of recombinant P. pastoris can significantly increase the titer of porcine myoglobin, so that the titer can reach 285.42 mg/L under fermenter conditions. In addition, by creatively adding different concentrations of ammonium sulfate to fermentation broth step by step, the purity of myoglobin obtained by final concentration is up to 88.0%, and the purification rate is up to 66.1%. The disclosure realizes efficient expression and high purification of porcine myoglobin from various steps such as synthesis, fermentation and purification of porcine myoglobin, and provides broad prospects for industrial production of porcine myoglobin.

Disclosed is a method for efficiently separating and purifying recombinant human coagulate factor VIII Fc fusion protein. The method comprises steps of affinity chromatography and anion exchange chromatography; and the sample captured by means of the affinity chromatography is eluted with a salt ion buffer containing 5%-20% polyol organic solvents under the condition of pH 4.0 to 8.0, and the protein sample can be separated and purified to 85% or more by further ProteinA affinity chromatography. The purification method is simple to operate, naturally connects each step of chromatography, has a high recovery rate and low cost, and easily increases production.

The present invention relates to monolithic bodies, uses thereof and processes for the preparation thereof. Certain embodiments of the present invention relate to the use of a monolithic body in the preparation of a radioactive substance, for example a radiopharmaceutical, as part of a microfluidic flow system and a process for the preparation of such a monolithic body.

The invention concerns a purification method comprising: providing a flow comprising a glycol, monovalent ions and multivalent ions; treating this flow with ion exclusion chromatography comprising: injecting the flow into a chromatographic unit comprising an ion exchange stationary phase; injecting an eluent into the chromatographic unit; collecting a fraction at the outlet of the chromatographic unit; the collected fraction being enriched with glycol and depleted of monovalent ions and multivalent ions relative to the flow.

The invention also concerns an installation adapted to implement this method, and its application to the regeneration of an anti-hydrate agent.