Methods for differentiating full-length high molecular weight kininogen (HMWK) and cleaved HMWK in a sample are provided herein. Such methods may comprise treating a biological sample with a protease to generate a plurality of digested peptides, and measuring one or more signature peptides, which are indicative of cleaved HMWK and/or full-length HMWK.

The present invention provides methods for improved label-free absolute quantification of relatively low abundant polypeptides by liquid chromatography/mass spectrometry analysis of peptide products obtained from simple or complex polypeptide mixtures. The methods for absolute quantification include MS signals from a set of qualified ions of peptide products of a relatively high abundant polypeptide to improve quantification of a relatively low abundant polypeptide.

Technologies for identifying one or more neoepitope peptides include generating a database that includes peptide sequences within a predefined range of length of residues, assigning a prior probability to each of the peptide sequences in the database, obtaining mass spectra of a plurality of fragments of a target molecule produced by mass spectrometry, determining, for each mass spectrum, matching scores of peptide-spectrum matches between the mass spectra and the peptide sequences in the database as a function of prior probabilities of the peptide sequences and matching probabilities, and determining a subset of the peptide-spectrum matches that has a corresponding matching score higher than a threshold.

The present invention provides assays and assay systems for use in spatially encoded biological assays. The invention provides an assay system comprising an assay capable of high levels of multiplexing where reagents are provided to a biological sample in defined spatial patterns; instrumentation capable of controlled delivery of reagents according to the spatial patterns; and a decoding scheme providing a readout that is digital in nature.

Bead-based analytical assays suitable for detecting changes in the abundance of target analytes in biological samples are disclosed. In an embodiment, an assay involves incubating a sample with one or several beads that are capable of binding several distinct analytes in an amount sufficient for detection by mass spectrometry from a single bead.

Among the various aspects of the present disclosure is the provision of compositions for and methods of diagnosing, prognosing, and treating diabetes.

A method includes applying distinct isobaric tags to each of a plurality of samples; combining the samples; performing a separation of species within the combined samples; isolating and fragmenting labeled parent ions within a m/z range to produce a plurality of reporter ions, each reporter ion corresponding to one of the isobaric tags; determining intensities of the plurality of reporter ions and ions representative of a parent species at a plurality of points along a peak; and fitting the intensity of the ions representative of a parent species and the plurality of reporter ions at the plurality of points to obtain a relative abundance of the parent species in each of the plurality of samples.

Methods to rapidly and accurately detect, characterize, measure, and quantify site-specific antibody drug conjugates, that may be present in pre-clinical animal biological samples, or human biological samples, including plasma/serum and tissue samples.

Aspects disclosed herein include a method for matching hair composition, the method comprising: characterizing one or more first characteristics of a natural melanin composition of a hair sample from a subject; and preparing a prepared artificial melanin formulation to approximate (or, to match or to resemble) the one or more first characteristics; wherein the prepared artificial melanin formulation comprises one or more artificial melanin materials.

Embodiments described herein provide a solution to the measurement of various dystrophins expressed in a cell or tissue. The solution to this problem is a specific and sensitive quantitative method to measure endogenous and/or exogenous dystrophin (e.g., engineered dystrophin) expression in skeletal muscle tissue, which provides a substantial benefit to drug development and monitoring of treatment.