Described are methods, compositions, and devices for a concatemeric protein standard that behaves as a protein but transforms into single peptides upon digestion, which is optimized to function as a non-obtrusive process control for mass spectrometry analysis.

The present invention provides a set of novel isobaric chemical tags, also referred herein as SUGAR (Isobaric Multiplex Reagents for Carbonyl Containing Compound). These labeling tags are compact and easy to synthesize at high yield and purity in just a few steps using commercially available starting materials. The tagging reagents of the present invention comprise: a) a reporter group, having at least one atom that is optionally isotopically labeled; b) a balancing group, also having at least one atom that is optionally isotopically labeled, and c) an aldehyde, ketone, or carboxylic acid reactive group. The multiplex SUGAR tags are able to react with an aldehyde, ketone, or carboxylic acid group of the molecule to be tagged, which offers the capability for labeling and quantitation of glycans, proteins/peptides, and fatty acids.

Apparatus, methods and kits for detecting the contamination of a meat sample with another type of meat using parent-daughter ion transition monitoring that identifies peptides specific to a particular type of meat. The meat types detected can include pork, beef, lamb, chicken, duck and/or horse and one or more combinations thereof.

This disclosure generally relates to embodiments for detecting presence of one or more allergens in mammalian milk. An exemplary embodiment relates to a method to detect presence of one or more allergen molecules in a composition of mammalian milk, the method includes the steps of: providing a substrate having a plurality of detection sites thereon, each of the plurality of detection sites configured to detect presence of one or more allergen molecules; exposing the plurality of detection sites to a quantity of mammalian milk; detecting presence of a first allergen molecule at a first of the plurality of detection sites by detecting a fragment of DNA, RNA, or amino acids corresponding to the first allergen molecule; wherein the detected fragment excludes naturally occurring molecules present in the composition of mammalian milk.

A method of analysis using mass spectrometry and/or ion mobility spectrometry is disclosed. The method comprises: using a first device to generate smoke, aerosol or vapour from a target comprising or consisting of a microbial population; mass analysing and/or ion mobility analysing said smoke, aerosol or vapour, or ions derived therefrom, in order to obtain spectrometric data; and analysing said spectrometric data in order to analyse said microbial population.

The present systems and methods introduce deep learning to de novo peptide sequencing from tandem mass spectrometry data. The systems and methods achieve improvements in sequencing accuracy over existing systems and methods and enables complete assembly of novel protein sequences without assisting databases. The present systems and methods are re-trainable to adapt to new sources of data and provides a complete end-to-end training and prediction solution, which is advantageous given the growing massive amount of data. The systems and methods combine deep learning and dynamic programming to solve optimization problems.

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 μM to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

The invention relates to a method of analyzing the metabolic content of a biological sample comprising: i) providing one or more samples of extracted metabolites from the biological sample; ii) performing a chromatography coupled mass spectrometry analysis of the extracted metabolites to generate a full raw data set for full scan ions; iii) generating a full data cluster set from the full raw data set obtained in step ii) by grouping full scan ions according to isotope and adduct values; iv) performing a tandem mass spectrometry analysis of the extracted metabolites with a plurality of mass selection windows to generate a raw SWATH® data set for fragment ions; v) generating a SWATH® data cluster set from the raw SWATH® data set obtained in step iv) by grouping fragment ions according to retention time and mass values; vi) aligning the SWATH® data cluster set with the full data cluster set to generate characteristic profile for each extracted metabolite; vii) comparing the data using R characteristic profile of each extracted metabolite obtained in step vi) with a reference library of characteristic profiles of metabolites to provide the metabolic content of the biological sample.

The present invention relates to a method for determining the distinctive nutritional requirements of a patient with specific nutritional needs and providing a composition meeting the distinctive nutritional requirements of said patient.

Use of a limited digestion with a proteolytic enzyme of a multispecific antibody for the analysis of the multispecific antibody's light chain pairing.