A channel bubble reduction device includes a liquid accommodation portion, that accommodates a liquid, a liquid supply apparatus that, with a pushing operation of a rod, discharges the liquid through an aperture portion of a tube portion, a first channel that connects the aperture portion of the liquid supply apparatus with the liquid accommodation portion, and an air layer formation apparatus that forms an air layer in at least one of the first channel or the tube portion.

In certain embodiments, the present invention provides a method of measuring the level of hydrophobicity of a chromatographic resin. In certain embodiments, the present invention provides a method of selecting a chromatographic resin condition for purifying a protein of interest from a mixture, wherein the protein of interest has low or no aggregation formation during chromatography. In certain embodiments, the present invention provides a method of selecting a chromatographic resin from a plurality of chromatographic resins for purifying a protein of interest from a mixture, wherein the protein of interest has low or no aggregation formation during chromatography.

In certain embodiments, the present invention provides a method of measuring the level of hydrophobicity of a chromatographic resin. In certain embodiments, the present invention provides a method of selecting a chromatographic resin condition for purifying a protein of interest from a mixture, wherein the protein of interest has low or no aggregation formation during chromatography. In certain embodiments, the present invention provides a method of selecting a chromatographic resin from a plurality of chromatographic resins for purifying a protein of interest from a mixture, wherein the protein of interest has low or no aggregation formation during chromatography.

An ion exchange chromatography column contains an ion exchange stationary phase that includes a charged substrate, a plurality of first particles, and a plurality of second particles. The plurality of first particles each include first ion exchange groups and the first particles are ionically bound to the charged substrate. The plurality of second particles each include second ion exchange groups and the second particles are ionically bound to the charged substrate. The first particles having a first ion exchange group density, and the second particles having a second ion exchange group density. The first ion exchange group density is greater than the second ion exchange group density. The ion exchange chromatography column has a number of zones connected in series where each zone can have a varying level of first ion exchange groups and second ion exchange group from the inlet zone to the outlet zone.

The invention provides methods for microbial bioburden reduction of various chromatography matrices, including bioburden reduction in the context of large-scale Protein A-based affinity chromatography columns.

The invention provides methods for microbial bioburden reduction of various chromatography matrices, including bioburden reduction in the context of large-scale Protein A-based affinity chromatography columns.

Provided herein are methods of reducing bioburden of a chromatography resin that include exposing a container including a composition including (i) a chromatography resin and (ii) a liquid including at least on alcohol to a dose of gamma-irradiation sufficient to reduce the bioburden of the container and the chromatography resin, where the at least one alcohol are present in an amount sufficient to ameliorate the loss of binding capacity of the chromatography resin after/upon exposure to the dose of gamma-irradiation. Also provided are reduced bioburden chromatography columns including the reduced bioburden chromatography resin, compositions including a chromatography resin and a liquid including at least one alcohol, methods of performing reduced bioburden column chromatography using one of these reduced bioburden chromatography columns, and integrated, closed, and continuous processes for reduced bioburden manufacturing of a purified recombinant protein.

The invention discloses a method for sanitization of a bioprocess chro matography column, comprising the steps of: a) providing a bioprocess chromatogra phy column with a packed bed of separation resin particles and a movable adapter, b) with the adapter in contact with the packed bed, conveying a sanitization fluid through the packed bed to a column outlet; c) raising the adapter to provide a gap between the packed bed and the adapter, d) lowering the adapter to close the gap; and e) conveying an equilibration liquid through the packed bed to a column outlet.

The invention discloses a method for sanitization of a bioprocess chro matography column, comprising the steps of: a) providing a bioprocess chromatogra phy column with a packed bed of separation resin particles and a movable adapter, b) with the adapter in contact with the packed bed, conveying a sanitization fluid through the packed bed to a column outlet; c) raising the adapter to provide a gap between the packed bed and the adapter, d) lowering the adapter to close the gap; and e) conveying an equilibration liquid through the packed bed to a column outlet.

Provided herein are methods for high throughput quantitation of testosterone utilizing at least two different derivatizing agents of different masses. In another aspect, provided herein are methods for determining the amount of testosterone in each of a plurality of human samples with a single mass spectrometric assay by subjecting each of a plurality of human samples to a different derivatizing agent to generate a differently derivatized testosterone in each of the plurality of samples; combining the plurality of samples to form a multiplex sample; and quantifying the amount of testosterone in each sample by mass spectrometry.