The present invention relates to a method of preparing a population of antibodies, whereby a desired high-purity and high-quality population of antibodies can be prepared by removing impurities without using an expensive protein A column, and in particular, production costs can be significantly reduced while achieving process automation; and a population of antibodies prepared thereby.

Aspects of the present disclosure relate to a method of regenerating a hydrophobic interaction chromatography column to which a load mass has been applied, the method comprising passing one or more column volumes of an alkaline solution through hydrophobic interaction media within the column, wherein the alkaline solution exhibits a pH of between about 10 and about 14, and a conductivity of between 0.5 mS/cm and about 10 mS/cm, wherein material bound to the hydrophobic interaction media is removed. In some cases, the alkaline solution may include sodium hydroxide at a concentration of between, e.g., about 0.1 mM and 10 mM.

Aspects of the present disclosure relate to a method of regenerating a hydrophobic interaction chromatography column to which a load mass has been applied, the method comprising passing one or more column volumes of an alkaline solution through hydrophobic interaction media within the column, wherein the alkaline solution exhibits a pH of between about 10 and about 14, and a conductivity of between 0.5 mS/cm and about 10 mS/cm, wherein material bound to the hydrophobic interaction media is removed. In some cases, the alkaline solution may include sodium hydroxide at a concentration of between, e.g., about 0.1 mM and 10 mM.

The present invention relates to a novel polypeptide affinity ligand coupled to solid supports and affinity purification of IgG antibodies. The invention is comprised of (1) the design, generation, and purification of polypeptide ligands, (2) coupling of a polypeptide affinity ligand to a solid support matrix, (3) purification of IgG (polyclonal and monoclonal antibodies), and (4) cleaning and reuse of polypeptide supported solid matrix.

Provided herein are methods of separating host cell lipases from an anti-LAG3 antibody or antigen binding fragment in chromatographic processes and methods of improving polysorbate-80 stability in an anti-LAG3 antibody formulation by separating host cell lipases from the anti-LAG3 antibody or antigen binding fragment using chromatographic processes. Also provided are pharmaceutical compositions comprising an anti-LAG3 antibody or antigen binding fragment and less than 2 ppm of a host cell lipase.

Provided herein are methods of separating host cell lipases from an anti-LAG3 antibody or antigen binding fragment in chromatographic processes and methods of improving polysorbate-80 stability in an anti-LAG3 antibody formulation by separating host cell lipases from the anti-LAG3 antibody or antigen binding fragment using chromatographic processes. Also provided are pharmaceutical compositions comprising an anti-LAG3 antibody or antigen binding fragment and less than 2 ppm of a host cell lipase.

Disclosed is a method for efficiently separating and purifying recombinant human coagulate factor VIII Fc fusion protein. The method comprises steps of affinity chromatography and anion exchange chromatography; and the sample captured by means of the affinity chromatography is eluted with a salt ion buffer containing 5%-20% polyol organic solvents under the condition of pH 4.0 to 8.0, and the protein sample can be separated and purified to 85% or more by further ProteinA affinity chromatography. The purification method is simple to operate, naturally connects each step of chromatography, has a high recovery rate and low cost, and easily increases production.

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.

A relatively fast, inexpensive, and non-destructive method for separation and isolation of biologically active nanoparticles is described. Methods include the use of solid phase separation medis such as channeled fibers in a hydrophobic interaction chromatography (HIC) protocol to isolate biologically active nanoparticles from other components of a mixture. Biologically active nanoparticles can include natural nanoparticles (e.g., exosomes, lysosomes, virus particles) as well as synthetic nanoparticles (liposomes, genetically modified virus particles, etc.)

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.