A solid phase for use in separation has been modified using an aqueous phase adsorption of a headgroup-modified lipid to generate analyte specific surfaces for use as a stationary phase in separations such as high performance liquid chromatography (HPLC) or solid phase extraction (SPE). The aliphatic moiety of the lipid adsorbs strongly to a hydrophobic solid surface, with the hydrophilic and active headgroups orienting themselves toward the more polar mobile phase, thus allowing for interactions with the desired solutes. The surface modification approach is generally applicable to a diversity of selective immobilization applications such as protein immobilization clinical diagnostics and preparative scale HPLC as demonstrated on capillary-channeled fibers, though the general methodology could be implemented on any hydrophobic solid support material.

A solid phase for use in separation has been modified using an aqueous phase adsorption of a headgroup-modified lipid to generate analyte specific surfaces for use as a stationary phase in separations such as high performance liquid chromatography (HPLC) or solid phase extraction (SPE). The aliphatic moiety of the lipid adsorbs strongly to a hydrophobic solid surface, with the hydrophilic and active headgroups orienting themselves toward the more polar mobile phase, thus allowing for interactions with the desired solutes. The surface modification approach is generally applicable to a diversity of selective immobilization applications such as protein immobilization clinical diagnostics and preparative scale HPLC as demonstrated on capillary-channeled fibers, though the general methodology could be implemented on any hydrophobic solid support material.

The present disclosure features a composition, including molecularly imprinted crosslinked polymers that have been imprinted with trimethylamine N-oxide. The molecularly imprinted crosslinked polymers have specific binding sites for trimethylamine N-oxide, and a trimethylamine N-oxide absorption capacity of at least 0.5 mg/g.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising at least 15 mg/ml multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support, wherein the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml; b) contacting a liquid sample comprising an immunoglobulin with the separation matrix; c) washing the separation matrix with a washing liquid; d) eluting the immunoglobulin from the separation matrix with an elution liquid; and e) cleaning the separation matrix with a cleaning liquid comprising at least 0.5 M NaOH.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising at least 15 mg/ml multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support, wherein the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml; b) contacting a liquid sample comprising an immunoglobulin with the separation matrix; c) washing the separation matrix with a washing liquid; d) eluting the immunoglobulin from the separation matrix with an elution liquid; and e) cleaning the separation matrix with a cleaning liquid comprising at least 0.5 M NaOH.

The invention relates to a separation matrix comprising at least 11 mg/ml Fc-binding ligands covalently coupled to a porous support, wherein: a) the ligands comprise multimers of alkali-stabilized Protein A domains, and b) the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml.

The invention relates to a separation matrix comprising at least 11 mg/ml Fc-binding ligands covalently coupled to a porous support, wherein: a) the ligands comprise multimers of alkali-stabilized Protein A domains, and b) the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml.

The present invention provides a chromatography medium comprising one or more electrospun polymer nanofibers which form a stationary phase comprising a plurality of pores through which a mobile phase can permeate and use of the same in chromatography, such as the isolation of recombinant proteins, monoclonal antibodies, viral vaccines and plasmid DNA. The invention further provides for the use of the chromatographic medium in a simulated moving bed system.

The present invention provides a chromatography medium comprising one or more electrospun polymer nanofibers which form a stationary phase comprising a plurality of pores through which a mobile phase can permeate and use of the same in chromatography, such as the isolation of recombinant proteins, monoclonal antibodies, viral vaccines and plasmid DNA. The invention further provides for the use of the chromatographic medium in a simulated moving bed system.

The invention relates to a method for the separation of two hydrophilic neutral oligosaccharides from each other with a chromatography on a bromine functionalized polystyrene cross-linked with divinylbenzene (BPS-DVB) stationary medium.