The present invention provides methods for performing supercritical fluid chromatography comprising loading a sample to be separated by supercritical fluid chromatography onto a stationary phase comprising a spherical, monodisperse, core-shell particulate material comprising a nonporous core and one or more layers of a porous shell material surrounding the core, wherein the particles are sized less than 2 microns; and performing supercritical fluid chromatography to separate the sample.

A mixed mode affinity chromatography carrier includes a substrate, a hydrophilic polymer, an antibody-binding cyclic peptide, and a cation exchange group.

A chromatography column for the use of separation of acidic sugar chains, wherein the column comprises a first column and a second column, the second column connected by a flow path downstream of an outlet of the first column, and selected from the following (1) or (2): (1) the carrier of the first column is hydrophobically modified silica having a group containing a primary amine, a secondary amine or/and a tertiary amine, and the carrier of the second column is a resin having a group containing a primary amine, a secondary amine or/and a tertiary amine; (2) the carrier of the first column is a resin having a group containing a primary amine, a secondary amine or/and a tertiary amine, and the carrier of the second column is hydrophobically modified silica having a group containing a primary amine, a secondary amine, or/and a tertiary amine.

Disclosed herein are embodiments of methods for oligonucleotide analysis using a novel solid-phase extraction and hydrophilic-interaction liquid chromatography. The unique polar-based retention methods provided herein provide a high-recovery extraction. The methods improve assay reliability and reproducibility and reach picomolar sensitivity with the demonstrably beneficial accurate mass platform. Also disclosed herein are systems and computer program products for performing these methods.

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 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 the determination of analytes in a sample using chromatography. The present disclosure provides methods of separating an analyte from a sample. A mobile phase is flowed through a chromatography column. The mobile phase includes about 0.005% (v/v) to about 2.50% (v/v) difluoroacetic acid and less than about 100 ppb of any individual impurity, especially metal impurities. A sample including the analyte is injected into the mobile phase. The analyte is separated from the sample.

The invention relates to poly-amide bonded hydrophilic interaction chromatography (HILIC) stationary phases and novel HILIC methods for use in the characterization of large biological molecules modified with polar groups, known to those skilled in the art as glycans. The invention particularly provides novel, poly-amide bonded materials designed for efficient separation of large biomolecules, e.g. materials having a large percentage of larger pores (i.e. wide pores). Furthermore, the invention advantageously provides novel HILIC methods that can be used in combination with the stationary phase materials described herein to effectively separate protein and peptide glycoforms by eliminating previously unsolved problems, such as on-column aggregation of protein samples, low sensitivity of chromatographic detection of the glycan moieties, and low resolution of peaks due to restricted pore diffusion and long intra/inter-particle diffusion distances.

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.

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.