A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

The present technology relates to a method of analyzing a sample including an analyte. The method includes injecting the sample including the analyte into a mobile phase. The mobile phase includes a metal chelator additive having a concentration between about 1 ppm to about 10 ppm. The method also includes separating the analyte using liquid chromatography and analyzing the analyte using a mass spectrometer, an ultra-violet detector, or a combination thereof.

A fluid mixer includes a flow splitter and a mixing chamber. The flow splitter includes an inlet for receiving a flow of fluid and is configured to split the flow of fluid into first and second fluid streams. The second fluid stream has a higher density than the first fluid stream. The mixing chamber includes a first inlet, a second inlet and a mixing well. The second inlet is positioned below the first inlet. The second inlet of the mixing chamber is configured to receive the first fluid stream and the first inlet of the mixing chamber is configured to receive the second fluid stream to promote mixing of the first and second streams in the mixing well.

Disclosed herein are methods and compositions for isolating a protein fraction from a potato sample. The methods include adjusting the potato sample containing the protein fraction to a pH of about 4.0 to 5.2; and loading the potato sample onto a sulfonated epoxy resin, wherein the sulfonated epoxy resin comprising Formula (I) is adjusted to a pH of about 4.0 to 4.5. The methods also include washing the sulfonated epoxy resin and eluting the protein fraction.

A method of operating a chromatography column is described. This method involves collecting column outlet signal and accumulated flow parameters at two or more intervals of at least one mobile phase transition front during operation of the chromatography column comprising column packing. A model gamma cumulative distribution curve is calculated based on the collected column outlet signal and accumulated flow parameters for the at least one mobile phase transition front. A height equivalent theoretical plate (HETP) value is calculated for the at least one mobile phase transition front using parameters of the model gamma cumulative distribution curve and the quality of the chromatography column packing is assessed based on the calculated HETP value.

The present invention provides a chromatographic separation method for improving the quality of albumin fusion protein solutions by removing impurities from the albumin fusion protein solution. This invention provides albumin fusion protein solution with a significantly reduced amount of the (yellow) coloured impurities and HCP.

The present disclosure relates to a nanoscale thin film structure and implementing method thereof, more specifically nanoscale thin film structure of which target structure is designed with quantized thickness and a method to implement the nanoscale thin film structure by which the performance of the manufactured nanodevice can be implemented the same as the designed performance, thereby applicable to high sensitivity high performance electronic/optical sensor devices.

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.