The present disclosure relates to, inter alia, a method of quantitating an amount of an antibody molecule from a mixture comprising two or more antibody molecules, comprising separating each of the two or more antibody molecules from the mixture by hydrophobic interaction chromatography high performance liquid chromatography (HIC-HPLC) and quantitating an amount of each antibody molecule, wherein the molecular weight of each antibody molecule is within 15 kDa of any other antibody molecule in the mixture and either each antibody molecule is different from another antibody molecule in the mixture by more than about 0.25 unit on the Kyte & Doolittle hydropathy scale or each of the antibody molecules when nm alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

The present disclosure relates to, inter alia, a method of quantitating an amount of an antibody molecule from a mixture comprising two or more antibody molecules, comprising separating each of the two or more antibody molecules from the mixture by hydrophobic interaction chromatography high performance liquid chromatography (HIC-HPLC) and quantitating an amount of each antibody molecule, wherein the molecular weight of each antibody molecule is within 15 kDa of any other antibody molecule in the mixture and either each antibody molecule is different from another antibody molecule in the mixture by more than about 0.25 unit on the Kyte & Doolittle hydropathy scale or each of the antibody molecules when run alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

Methods of purification and/or viral deactivation of a protein (e.g. glycoprotein) comprising a step of treating the protein (e.g. glycoprotein) with a combination of caprylic acid and ethanol.

The present invention relates generally to compositions for use in biological and chemical separations, as well as other applications. More specifically, the present invention relates to hybrid felts fabricated from electrospun nanofibers with high permeance and high capacity. Such hybrid felts utilize derivatized cellulose, and at least one non-cellulose-based polymer that may be removed from the felt by subjecting it to moderately elevated temperatures and/or solvents capable of dissolving the non-cellulose-based polymer to leave behind a porous nanofiber felt having more uniform pore sizes and other enhanced properties when compared to single component nanofiber felts.

The present invention relates to a method for preparing a composition comprising monomeric conjugates from a sample, said conjugate comprising (a) a polypeptide comprising the amino acid sequence of interleukin 15 or derivatives thereof, and (b) a polypeptide comprising the amino acid sequence of the sushi domain of IL-15R or derivatives thereof; wherein said method comprises the use of anion-exchange chromatography followed by a hydrophobic interaction chromatography; and to a pharmaceutical composition which can be obtained by such a method.

The present invention relates to a method for preparing a composition comprising monomeric conjugates from a sample, said conjugate comprising (a) a polypeptide comprising the amino acid sequence of interleukin 15 or derivatives thereof, and (b) a polypeptide comprising the amino acid sequence of the sushi domain of IL-15R or derivatives thereof; wherein said method comprises the use of anion-exchange chromatography followed by a hydrophobic interaction chromatography; and to a pharmaceutical composition which can be obtained by such a method.

This invention relates to a hybrid ligand, a hybrid biomimetic chromedia and a preparing method and a use thereof, wherein the hybrid biomimetic chromedia takes hydrophilic porous microsphere as a substrate in chromatography, activated with allyl bromide and undergoing bromo-alcoholization with N-bromosuccinimide, then coupled with the hybrid ligands. The sequence of the hybrid ligand is phenylalanine-tyrosine-glutamine-5-aminobenzimidazole. The hybrid biomimetic chromedia has both of the two functional groups of phenylalanine-tyrosine-glutamine tripeptide and aminobenzimidazole, while maintaining the high antibody selectivity of polypeptide ligand, hydrophobic electric charge inductive ligand is introduced to achieve more moderate elution requirement, realizing effective antibody separation.

A method of separating biomolecules in an aqueous mixture is disclosed comprising a obtaining a separation vessel containing separation media, wherein the separation media comprises a porous support with a hydrophobic monomer grafted thereon, the hydrophobic monomer having the structure:

CH.sub.2CR.sup.4C(O)NHC(R.sup.1R.sup.1)(C(R.sup.1R.sup.1)).sub.nC(O)XR.sup.3

wherein n is an integer of 0 or 1; R.sup.1 is independently selected from at least one of: a hydrogen atom, alkyls, aryls, and alkylaryls, wherein the alkyls, aryls, and alkylaryls have a total of 10 carbon atoms or less; R.sup.3 is a hydrophobic group selected from at least one of alkyls, aryls, alkylaryls and ethers, wherein the alkyls, aryls, alkylaryls and ethers have a total number of carbon atoms ranging from 4 to 30; R.sup.4 is H or CH.sub.3; and X is O or NH; wherein the hydrophobic monomer is derived from an amine or an alcohol (HXR.sup.3) that has a hydrophilicity index of 25 or less; and
(b) passing the aqueous mixture through the separation vessel thereby separating the biomolecules. Such methods can be used to separate proteins, antibodies, fusion proteins, vaccines, peptides, enzymes, DNA, and/or RNA.

Chromatography resins having anionic exchange-hydrophobic mixed mode ligands, that are useful for purifying target biomolecules using anionic exchange (i.e., where the ligand is positively charged) and hydrophobic mixed mode chromatography. The chromatography resins allow for efficient purification of target biomolecules (e.g., recombinant proteins, antibodies, antibody-drug conjugates, or antibody derivatives including, but not limited to, antibody fragments and antibody fusions) from a sample, and have been found to be useful in purifying monomeric target biomolecules from aggregate target biomolecules. In an embodiment, the chromatography resins are useful for separating antibodies from one or more components (e.g., contaminants) in the sample.

Chromatography resins having anionic exchange-hydrophobic mixed mode ligands, that are useful for purifying target biomolecules using anionic exchange (i.e., where the ligand is positively charged) and hydrophobic mixed mode chromatography. The chromatography resins allow for efficient purification of target biomolecules (e.g., recombinant proteins, antibodies, antibody-drug conjugates, or antibody derivatives including, but not limited to, antibody fragments and antibody fusions) from a sample, and have been found to be useful in purifying monomeric target biomolecules from aggregate target biomolecules. In an embodiment, the chromatography resins are useful for separating antibodies from one or more components (e.g., contaminants) in the sample.