The invention provides a container for storing a biomaterial in which adhesion of a minute amount of a biomarker(s) contained in the biomaterial to the surface of the container for storage can be suppressed, and sample loss is reduced, while enabling analysis with accuracy and highly precision. In particular, the container for storing a biomaterial for reducing sample loss of a biomarker(s) contained in the biomaterial has a coating containing a copolymer which contains a recurring unit which contains a group represented by the following formula (a), a recurring unit which contains a group represented by the following formula (b), and optionally a recurring unit which contains a group represented by the following formula (c), on at least a part of the surface of the container:

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(wherein, U.sup.a1, U.sup.a2, U.sup.b1, U.sup.b2 and U.sup.b3, An.sup.− and R.sup.c are as defined herein).

The present invention relates to the use of a particle, including a virus-like particle (VLP), for the discovery and analysis of protein-protein interactions that are modulated by small molecules.

A method for increasing peptide fragmentation by labelling the peptide at the C-terminal end with a guanidinium group or other basic functional group and distinguishing isobaric amino acids and amino acid combinations of asparagine and glycine-glycine; glutamine and glycine-alanine; and/or glutamine and alanine-glycine, during polypeptide sequencing. The method involves: obtaining a peptide of interest and/or digesting a polypeptide of interest with a protease, such as pepsin, chymotrypsin or trypsin, or by chemical cleavage to produce shorter peptides; reacting the obtained and/or generated peptides with a coupling reagent to derivatize the free C-terminal carboxylic acid function of the peptides, thus adding a basic functional group rendering C-terminal peptide fragment ions detectable by mass spectrometry; selecting a charge state of 2+ or more, and fragmenting the derivatized peptides in a mass spectrometer under conditions effective to generate at least w ions; and detecting the w ions by mass spectrometry, and identifying derivatized peptides which incorporate the additional mass of the basic functional group.

A method for preparing an analytical sample for analyzing a glycan contained in a sample includes: performing a first reaction so that when sialic acid is linked to the glycan, sialic acid of a first linkage type is lactonized and modification different from lactonization is performed on sialic acid of a second linkage type different from the first linkage type; performing a second reaction to ring-open a lactone formed in the first reaction; and performing the first reaction again.

A method for characterizing or quantifying one or more proteins in visible and/or sub-visible particles formed in a sample by detecting the at least one visible or sub-visible particle in the sample, isolating and capturing the at least one visible or sub-visible particle to identify a presence of a protein, and using a mass spectrometer to characterize the protein.

This disclosure relates to a virus-like particle in which a small molecule-protein complex is entrapped, ensuring the formation of the small molecule-protein complex under physiological conditions, while protecting the small molecule-protein complex during purification and identification. The disclosure further relates to the use of such virus-like particle for the isolation and identification of small molecule-protein complexes.

The present disclosure provides a biosignature that distinguishes Lyme disease, including early Lyme disease, from STARI. The present disclosure also provides methods for detecting Lyme disease and STARI, as well as methods for treating subjects diagnosed with Lyme disease or STARI.

Provided are methods for detecting chromogranin A by mass spectrometry. In another aspect, provided herein are methods for quantitating chromogranin A by mass spectrometry. In another aspect, provided herein are methods for prognosis of or measuring the size of neuroendocrine tumors by mass spectrometry.

Methods are provided for assessing risk of developing esophageal adenocarcinoma in a subject using one or more of the following marker genes/proteins: ISG15, LTF, CNDP2, DAD1, SET, UBE2N, S100P, and GPI. Methods are also provided for determining expression of one or more esophageal adenocarcinoma risk factors in a subject. Methods are also provided for treating esophageal adenocarcinoma in a subject, for preventing esophageal adenocarcinoma in a subject, for inhibiting or decreasing proliferation of esophageal adenocarcinoma cells, for inhibiting or decreasing migration of esophageal adenocarcinoma cells, or for increasing susceptibility to cytotoxicity or inducing cell death of esophageal adenocarcinoma cells.

In some embodiments, a mass spectrometry tag may comprise a linker region, a mass balance region, and a reporter region. The mass spectrometry tag may be configured to fragment in a mass spectrometer via an energy dependent process to produce multiple reporter molecules. For example, the reporter region of the tag may be configured to produce at least two reporter molecules via fragmentation. In some embodiments, one or more regions of the tag may comprise at least one heavy isotope. In some such embodiments, the ability to fragment into multiple reporter molecules as well as the placement and/or number of heavy isotope(s) allows the mass spectrometry tag to be distinguished from other similar mass spectrometry tags. In some such embodiments, the ability to distinguish between tags having the same or substantially similar total mass to charge ratio and reporter region mass may allow the system to have a greater multiplexing capacity than conventional systems.