Methods of detecting and quantifying target molecules, such as proteins, in a biological sample are provided. The disclosed methods include capturing target molecules with aptamers, replacing the aptamers with aptamer identification sequences, and then sequencing the aptamer identification sequences using next-generation sequencing techniques.

The subject invention provides methods for fabricating electrochemical aptamer-based (E-AB) sensors with enhanced sensitivity, signal-to-noise ratios, LOD, and improved stability and reproducibility. The subject invention also provides methods for aptamer immobilization on the surface of the electrode, which favors sufficient spacing between aptamers at the microscale to achieve optimal target recognition, folding, and signal transduction. The E-AB sensors of the subject invention provide superior sensing regardless of the sequence or structure of the bound aptamers or the physiochemical properties of the target.

In various embodiments methods are provided for identifying a mammal having an elevated risk for an adverse cardiac event (e.g. an MI) and/or determining the prognosis for the mammal. In certain embodiments the methods comprise determining, or causing to be determined, the presence and/or level of antibodies that bind a malondialdehyde acetaldehyde adduct (MAA adduct) in a biological sample from the mammal, where an elevated level of anti-MAA adduct antibodies, as compared to the level found in a normal healthy mammal is an indicator that that said mammal has one or more atherosclerotic lesions and/or is at elevated risk for a myocardial infarction.

The present invention provides a method for capturing a candidate substance that can bind to a complex of a MR1 protein and a β2 microglobulin protein more widely. A method for capturing a candidate substance that can bind to a complex of a MR1 protein and a β2 microglobulin protein of the present invention includes steps of: forming a complex of the test substance, the MR1 protein, and the β2 microglobulin protein by causing the test substance, the MR1 protein, and the β2 microglobulin protein to coexist; and reducing the complex with a reducing agent.

Provided is a stress measurement system and a stress measurement method that are capable of measuring the stress level of a subject without taking time and effort. A stress measurement system 1 includes a sensor unit 31 that detects a plurality of detection target gases based on substances contained in a specimen of a subject and outputs a plurality of detection values corresponding to respective detection results of the plurality of detection target gases, and a control unit that determines a stress level of the subject, based on a combination of the plurality of detection values. In addition, the substances contained in the specimen may include a substance serving as a raw material for a brain neurotransmitter.

Methods of assessing an analyte in a blood sample are provided according to aspects of the present disclosure which include: extracting the analyte from a biological sample dried on a treated support, producing an extracted sample, the treated support comprising a protein denaturant, wherein the analyte is a substrate for an enzyme present, or suspected of being present, in the biological sample, wherein the protein denaturant inhibits enzymatic activity of the enzyme on the analyte; and subjecting the extracted sample to liquid chromatography tandem mass spectrometry (LC/MS/MS), thereby assessing the analyte in the biological sample.

The invention provides methods of testing food for antigens that are more stable to food processing than more clinically problematic allergens from the same food. When clinically-significant allergens are disproportionately broken down by common preparation methods, the presence of certain food ingredients may be “masked” to some tests yet may still be allergenic. To prevent false negative results due to food preparation, the invention provides tests that test for specific food antigens that are selected on the basis of their stability under processing. Antigens are selected for inclusion in the test not because they are the most clinically relevant allergens, but rather because they are robust to processing (e.g., and do not denature during cooking). Tests of the invention may also test for the most clinically relevant allergens, but importantly, by testing for stable protein products/antigens, the tests report the presence of food residues even after commercial processing.

The present disclosure provides, inter alia, methods and compositions (e.g., conjugates) for imaging, at high spatial resolution, targets of interest.

Described herein are aptamers capable of binding to growth differentiation factor 11 (GDF11) protein; compositions comprising a GDF11 binding aptamer with a GDF11 protein; and methods of making and using the same.

Embodiments disclosed include systems, devices, and methods for analysis of samples containing particles used for gene delivery to determine a quality of the sample and/or an indication that the gene delivery particles are in a full, partial, and/or empty state. The present disclosure also relates to determining a protein and/or NA content in samples with known proportions of gene delivery particles in a full, partial, and/or empty state and based on the determination, establish a relationship between NA content and proportions of gene delivery particles in a full state. The present disclosure also relates to using such an established relationship to predict a proportion of the gene delivery particles in a full, partial, and/or empty state in test samples having the gene delivery particles in an unknown state.