A fluid analyzer for analyzing fluid samples comprising one or more analytes and a method of calibrating such. The fluid analyzer includes a control system to control at least one automated valve to pass at least three calibration reagents through a fluid channel to a secondary ion selective electrode, a primary ion selective electrode, and a reference electrode, and determine calibration information using calibration logic from signals generated by a meter, control the at least one automated valve to selectively pass different subsets of the at least three calibration reagents through the fluid channel to the secondary ion selective electrode, the primary ion selective electrode, and the reference electrode, and determine re-calibration information using the signals generated by the meter and at least one of the calibration information and re-calibration logic.

Provided herein are novel compounds, compositions, that can used as clickable, photo-affinity labeling (PAL) probes methods for use in screening NAD+ binding proteins.

The present invention relates to enzyme inhibitors. More specifically, the present invention relates to ligand-directed covalent modification of proteins; method of designing same; pharmaceutical formulation of same; and method of use.

The present invention relates to enzyme inhibitors. More specifically, the present invention relates to ligand-directed covalent modification of proteins; method of designing same; pharmaceutical formulation of same; and method of use.

Embodiments of the current disclosure are directed to systems, methods and apparatus for evaluating single cell secretion profiles. In some embodiments, the apparatus may be configured to analyze substances expressed by a biological cell and may include a first compressible substrate, and a second substrate configured for removable sealing attachment with the first substrate. In some embodiments, upon attachment of the second substrate with the first substrate, an assembly is formed such that the open side of the plurality of chambers are covered by the second substrate, and a portion of each of the plurality of capture areas are exposed in each of the chambers.

Described are methods for developing treatment plans for patients with cancer and other diseases based on drug binding interactions of kinase inhibitors. Also described are methods for determining the mutational status of a kinase and kinase occupancy.

The present invention provides a method for controlling a speed of a polypeptide passing through a nanopore and use thereof in determining an amino acid sequence of a polypeptide. Specifically, the method comprises: conjugating a polynucleotide to the polypeptide to give a polynucleotide-polypeptide conjugate, and applying a voltage across the nanopore in the presence of a polynucleotide binding enzyme to move the conjugate through the nanopore. The polynucleotide binding enzyme controls the movement of the polynucleotide and thereby controls the movement of the conjugated polypeptide in the nanopore, thus controlling the speed of the polypeptide passing through the nanopore. While controlling the speed of the polypeptide, the present invention reads a nanopore current signal during the process of the polypeptide passing through the nanopore to give an electrical signal of the polypeptide. The electrical signal can be further used to acquire an amino acid sequence of the polypeptide, to identify the polypeptide or a part thereof, or to establish a library of polypeptide electrical signals.

Embodiments of the current disclosure are directed to systems, methods and apparatus for evaluating single cell secretion profiles. In some embodiments, the apparatus may be configured to analyze substances expressed by a biological cell and may include a first compressible substrate, and a second substrate configured for removable sealing attachment with the first substrate. In some embodiments, upon attachment of the second substrate with the first substrate, an assembly is formed such that the open side of the plurality of chambers are covered by the second substrate, and a portion of each of the plurality of capture areas are exposed in each of the chambers.

Cyclic-GMP-AMP synthase (cGAS) and cyclic-GMP-AMP (cGAMP), including 2′3-cGAMP, 2′2-cGAMP, 3′2′-cGAMP and 3′3′-GAMP, are used in pharmaceutical formulations (including vaccine adjuvants), drug screens, therapies, and diagnostics.

Cyclic-GMP-AMP synthase (cGAS) and cyclic-GMP-AMP (cGAMP), including 2′3-cGAMP, 2′2-cGAMP, 3′2′-cGAMP and 3′3′-GAMP, are used in pharmaceutical formulations (including vaccine adjuvants), drug screens, therapies, and diagnostics.