A protein purification process with virus inactivation or removal uses caprylic acid (octanoic acid) at acidic pH. The method comprises caprylic acid treatment as part of the chromatographic step so as to perform viral inactivation without a discontinuous process and without the requirement of attention by personnel, particularly when the pH adjustment of the eluate is performed automatically by eluting into buffer. The method of the invention further results in mycoplasmas being inactivated, and reduced impurities like Host Cell Protein (HCP).

The invention provides methods for quantifying a non-ionic surfactant in a composition comprising a polypeptide and the non-ionic surfactant, where the quantification exhibits reduced interference between the non-ionic surfactant and the polypeptide. Also provided are methods where the composition further includes N-acetyl tryptophan, and the quantification exhibits reduced interference between the non-ionic surfactant, the polypeptide, and N-acetyl tryptophan.

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.

In various aspects, the present disclosure pertains to methods of performing a sample enrichment procedure, which comprise: adding a sample fluid that comprises at least one phospholipid and at least one target analyte to a sorbent that comprises a hydrophobic component and a cation exchange component, thereby resulting in sorbent with bound phospholipid and bound target analyte; adding an aqueous solution comprising an acidic compound and a salt; adding an organic solution to the sorbent thereby desorbing at least a portion of the bound phospholipid from the sorbent; and adding an elution solution to the sorbent, thereby desorbing at least a portion of the bound target analyte from the sorbent and forming a solution of the target analyte in the elution solution. In other aspects, the present disclosure pertains to kits, which may be used in conjunction with such methods.

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 provides methods for quantifying a non-ionic surfactant in a composition comprising a polypeptide and the non-ionic surfactant, where the quantification exhibits reduced interference between the non-ionic surfactant and the polypeptide. Also provided are methods where the composition further includes N-acetyl tryptophan, and the quantification exhibits reduced interference between the non-ionic surfactant, the polypeptide, and N-acetyl tryptophan.

An object of the present invention is to suppress the variation of the elution position of a compound having a charged portion by a preservation liquid, in the purification of the compound, without carrying out the substitution step of the preservation liquid attached to the adsorbent used for the purification and the keeping step. A method for purifying a compound having a charged portion, the method comprising the steps of: preparing a composition containing a compound having a charged portion; preparing a buffer solution comprising a buffering agent and an alcohol, the buffer containing a calcium phosphate compound at least partially, having a buffer capacity in a range of pH 6.0 to pH 8.0, and being soluble in a polar solvent and insoluble in a non-polar solvent; preserving an adsorbent in the buffer solution; adsorbing the compound on the adsorbent by bringing the composition into contact with the adsorbent preserved in the buffer solution; and separating the compound from the adsorbent by gradient elution.

Chromatography resins having mixed mode ligands and methods of using such resins are provided.

The present invention relates to a multimodal adsorption medium, in particular a multimodal chromatography medium, a method for its production, as well as use of the adsorption medium according to the invention or an adsorption medium produced according to the invention for the purification of biomolecules.

Disclosed is a method for filtering a fibrinogen composition, comprising the following steps: a) purifying the fibrinogen composition by chromatographic purification using an elution buffer comprising arginine; b) optionally, at least one step of filtering the fibrinogen composition obtained by chromatographic elution in step a), on a filter having a pore size of between 0.08 μm and 0.22 μm, c) filtering the fibrinogen composition obtained by chromatographic elution in step a), or optionally obtained in step b), on a symmetrical filter having a pore size of between 15 nm and 25 nm, and preferably between 18 nm and 22 nm, and d) recovering the resulting fibrinogen solution, the filtering method being carried out without adding arginine after step a), at a high capacity and without a prior freezing and/or thawing step.