Patent classifications
G01N27/44747
PREPARATIVE ELECTROPHORETIC METHOD FOR TARGETED PURIFICATION OF GENOMIC DNA FRAGMENTS
A sample containing particles having high-molecular-weight (HMW) DNA is entrapped in a gel matrix, and the gel matrix is exposed to a lysis reagent configured to release the HMW DNA from the particles. The HMW DNA may be purified by subjecting the gel matrix to an electrophoretic field that removes the HMW DNA from the particles, lysis reagents, and/or other sample constituents, from the gel matrix such that the HMW DNA remains. The gel matrix may be subjected with DNA cleavase reagents configured to cleave at specific DNA sequences within the HMW DNA to liberate defined segments of the DNA as fragments of reduced size. The gel matrix may also be subjected to an electrophoretic field, which moves and separates the DNA fragments from uncleaved DNA of the HMW DNA, which remains substantially immobile. The electrophoretically separated DNA fragments may be isolated from the gel matrix.
Microchip capillary electrophoresis assays and reagents
MCE assays and reagents to assess purity and to identify impurities in protein drug product samples are provided. Methods for analyzing analytes in a protein drug sample are provided.
METHOD OF PURITY DETERMINATION BY CAPILLARY ELECTROPHORESIS
Protein separation by capillary electrophoresis using a buffer composition comprising hydrophobic detergents that have alkyl chains longer than 12 carbon atoms. The formation of high molecular weight artifacts is suppressed.
Mass Spectrometer
An isotope ratio mass spectrometer has an ion source, a static field mass filter, a reaction cell to induce a mass shift reaction, and a sector field mass analyser for spatially separating ions from the reaction cell according to their m/z. A detector platform detects a plurality of different ion species separated by the sector field mass analyser. The static field mass filter has a first Wien filter that deflects ions away from a longitudinal symmetry axis of the spectrometer in accordance with the ions' m/z, and a second Wien filter that deflects ions back towards the longitudinal symmetry axis in accordance with the ions' m/z. An inverting lens is positioned along the longitudinal axis between the Wien filters to invert the direction of deflection of the ions from the first Wien filter. The static field mass filter provides high transmission and improved spectrometer sensitivity. The first and second Wien filters permit simple tuning.
ELECTROPHORESIS ASSEMBLY
This invention provided an electrophoresis assembly, comprising: a first plate; a second plate, being disposed substantially parallel to the first plate, in which a space is formed between the first plate and the second plate; a gel, being filled in the space between the first plate and the second plate; and at least one gel-support, being installed in the space at a predetermined position between the first plate and the second plate, wherein the gel-support is in tight combination with the gel for supporting the gel. The gel-support provide the gel support in the absence of the first plate or the second plate, and thus prevent a user tearing the gel when transferring the gel from a precast or other casted gel setting to other media.
Sample Component Separation Analysis Method
There is provided a separation analysis method for analyzing a sample component s included in a sample liquid by introducing the sample liquid into a separation flow path filled with a flow path liquid, the method comprising: obtaining a correction factor representing a proportion of a time period from the first point in time when the sample liquid is introduced into the separation flow path, to the second point in time when an interface between the flow path liquid and the sample liquid reaches a predetermined position at the separation flow path, with respect to a time period from the first point in time to the third point in time when an optical characteristic value of the sample component is measured at the predetermined position, and correcting the measured optical characteristic value with the correction factor.
Fiber coated nanopores
Provided herein are compositions, compounds, processes, and methods of use of 3D porous coating(s) on or near a nanopore(s) for analysis or detection of charged polymers such as nucleic acids, proteins, protein-nucleic acid complexes, small molecule-biological complexes, polymer-biological complexes, and/or polyelectrolytes.
Devices and methods using pore size modulation for detecting analytes in a fluid sample
Provided are devices that include a polymeric separation medium configured to immobilize one or more constituents of interest in the polymeric separation medium and have an increased pore size upon application of an applied stimulus. Systems including the devices, as well as methods of using the devices, are also provided. Embodiments of the present disclosure find use in a variety of different applications, including detecting whether an analyte is present in a fluid sample.
Use of Tri- and Tetra- Hydroxyl Quaternary Ammonium Compounds As Resolving Agents for Electrophoretic Separations
The present disclosure provides methods of improving the resolution of analytes by in electrophoretic separations using a gel by incorporating into the gel an effective amount of one or more tri- or tetra-hydroxyl quaternary ammonium compounds, or a mixture of such compounds.
Acid labile surfactants
This invention relates to an acid labile surfactant. In particular, the surfactants of the present invention include a dioxolane or dioxane functional group which enables the surfactant to hydrolyze in an acidic environment. Surfactants of this type can be utilized to enhance protein solubilization/enzyme digestion. Following hydrolysis to destroy the surfactant (which may chromatographic issues), there are generally two components formeda hydrophilic one, and a hydrophobic one. By altering the chemistry of the hydrolysable linker, the polarity of the hydrophobic residue can be altered, allowing it to be solubilized by significantly less organic solvent, and to minimize the potential loss of peptide material and to expand the chromatographic conditions that can be utilized.