A chemical analysis apparatus that quantitatively determines an object of detection rapidly with high sensitivity, and a pretreatment apparatus and a chemical analysis method used for the chemical analysis apparatus, are provided. The chemical analysis apparatus includes a pretreatment unit that accommodates a molecularly imprinted polymer capable of capturing a polar group-containing molecule included in a specimen. A quantification unit quantitatively determines a component included in the specimen that has been passed through the pretreatment unit.

The present invention relates to variant SH2 domains for binding a phosphotyrosine (pTyr)-containing peptide. The variant SH2 domains of the present invention include a parent SH2 domain having at least one amino acid substitution in a pre-defined region of 15 amino acid positions of the parent SR2 domain, wherein said at least one amino acid substitution increases the affinity of the variant SH2 domain for the pTyr-containing peptide relative to the parent SH2 domain. The present application relates also to methods of using the variant SH2 domains in the treatment of protein kinase-associated disorders, or the diagnosis or prognosis of protein kinase-associated disorders, for isolating and measuring the concentration of pTyr-containing molecules, and as reagents in research.

The present invention provides a method for providing a diagnosis or prognosis of a non-alcoholic fatty liver disease (NAFLD) in a subject by detecting expression level of the Squalene Epoxidase (SQLE) gene. A kit and device useful for such methods are also provided. In addition, the present invention provides a method for treating NAFLD by suppressing SQLE gene expression or activity.

There is provided a method of manufacturing a protein array or peptide array suitable for an efficient screening of a functional protein or functional peptide. The method of manufacturing a protein array or peptide array includes the steps of: (a) preparing a nucleic acid immobilized on a solid support and a cell-free synthesis system in a reactor, in which a reactor array includes the reactor having a specific aperture shape and a protein capture molecule or a peptide capture molecule provided on at least a portion of wall surface and bottom surface in the reactor; and (c) synthesizing a protein or peptide from the nucleic acid using the cell-free synthesis system and immobilizing the protein or peptide in the reactor.

The present invention relates to a method for identifying endogenous first responder protein-cysteines. Methods for screening candidate compounds suitable for regulating NF-kB signaling and the DNA damage response pathway are also disclosed.

One or more cells are labeled with minor stable isotopes, characterized, and preserved for subsequent use as a bio-specimen reference standard. The one or more cells are grown in culture media supplied with minor stable isotopes in concentrations substantially different from normally occurring concentrations, thereby supplanting major stable isotopes that would normally be incorporated into the proteins of the cells. The proteins of the cells are thus labeled by the minor stable isotopes and can be used in protcomic characterization of the cells. The cells are preserved by fixation as a reference standard. Cells of the reference standard are mixed with the sample and subject to mass spectrometry evaluation, whereby the labeled proteins of the reference standard can be used in determining the proteome of the sample.

Multiplexed test measurements are conducted using an assay module having a plurality of assay domains. In preferred embodiments, these measurements are conducted in assay modules having integrated electrodes with a reader apparatus adapted to receive assay modules, induce luminescence, preferably electrode induced luminescence, in the wells or assay regions of the assay modules and measure the induced luminescence.

The present invention provides compositions and methods that can be used to determine a peptide signature for an antibody repertoire in a sample comprising multiple antibodies. The method can be used to characterize a phenotype in a sample, such as providing a diagnosis, prognosis or theranosis of a medical condition.

The present invention relates to a method for the absolute quantification of naturally processed HLA-restricted cancer peptides, i.e. the determination of the copy number of peptide(s) as presented per cell. The present invention can not only be used for the development of antibody therapies or peptide vaccines, but is also highly valuable for a molecularly defined immuno-monitoring, and useful in the processes of identifying of new peptide antigens for immunotherapeutic strategies, such as respective vaccines, antibody-based therapies or adoptive T-cell transfer approaches in cancer, infectious and/or autoimmune diseases.

The present invention relates to: a newly developed triazine-cored amphiphilic compound; a preparation method therefor; and a method for extracting, solubilizing, stabilizing, crystallizing or analyzing membrane proteins by using the same. In addition, the compound enables membrane proteins, which have various structures and characteristics, to be efficiently extracted from cell membranes and stably stored in an aqueous solution for a long time, compared to a conventional compound, thereby being usable in functional and structural analysis thereof. Analyzing the structure and function of membrane proteins is closely related to the development of a novel drug, and thus is one of the greatest interests in the biology and chemistry fields.