In some aspects, the present disclosure pertains to sample treatment methods that comprise: contacting an acidic elution solution that is free of primary amine, secondary amine and thiol groups with a sorbent having bound target antibody and separating the elution solution from the sorbent, thereby releasing bound target antibody from the sorbent and forming a first collection fraction that comprises the elution solution and released target antibody; contacting the sorbent with a neutralization buffer solution that is free of primary amine, secondary amine and thiol groups and separating the neutralization buffer solution from the sorbent, thereby forming a second collection fraction that comprises the neutralization buffer solution; and forming a neutralized solution that comprises the first collection fraction and the second collection fraction. In other aspects, the present disclosure pertains to kits for performing such sample treatment methods.

The present disclosure relates to aflibercept, in particular, attributes of aflibercept. Also provided herein are methods of characterizing and modifying the attributes of aflibercept and compositions comprising aflibercept with particular attributes.

The present invention provides methods for purifying a polypeptide from a composition comprising the polypeptide and at least one contaminant and formulations comprising the polypeptide purified by the methods. The methods for purifying include cation exchange material and/or mixed mode material.

The present invention relates to a process for purification a protein comprising a semi-continuous chromatography step whereby the flow-through is collected and re-loaded onto the chromatography matrix.

The present invention provides methods for purifying a polypeptide from a composition comprising the polypeptide and at least one contaminant by overloading a chromatography material and eluting the product.

Provided herein are methods of purifying polypeptides comprising a circularly permuted interleukin-2 (IL-2) fused to the extracellular portion of an IL-2Rα chain.

The present invention provides a process for preparing a functionalised polymeric chromatography medium, which process comprises (I) providing two or more non-woven sheets stacked one on top of the other, each said sheet comprising one or more polymer nanofibres, (II) simultaneously heating and pressing the stack of sheets to fuse points of contact between the nanofibres of adjacent sheets, and (III) contacting the pressed and heated product with a reagent which functionalises the product of step (II) as a chromatography medium.

A mixed mode chromatography method for separating correctly folded from incorrectly folded conformations of a given protein is provided. The method is highly effective in separating correctly folded etanercept from incorrectly folded etanercept and aggregates in commercially attractive yields capable of affording etanercept preparations having very high purity in terms of correctly folded etanercept versus incorrectly folded etanercept. The invention is further directed to protein preparations and formulations comprising correctly folded proteins obtained using the present methods, and methods of treatment using the high purity preparations obtained from the mixed mode method.

A method for purifying a glycosylated recombinant protein of interest from a contaminant is disclosed that is suitable for industrial production purposes to remove galectins and other host cell contaminants, such as metallic cations, from recombinant therapeutic proteins.

A process for the production of a membrane protein including the steps of: expressing a membrane protein in a host organism present in an aqueous medium, liberating the membrane protein from the host organism, adding a detergent solution to solubilize the membrane protein, recovering a liquid fraction of the solubilized membrane protein, subjecting the liquid fraction to chromatography to bind or retain the membrane protein on a stationary phase, and eluting the stationary phase with an elution buffer to produce the membrane protein. The process can produce relatively large amounts of membrane proteins in an efficient way without including the quality of the end product.