Proteinuria markers and methods for their use are provided. These markers find many uses, including in diagnosing proteinuria, and treating proteinuria. In addition, reagents, devices and kits thereof that find use in practicing the subject methods are provided.

The present invention concerns a method for determining the concentration of a protein in a gastrointestinal (GI) tract sample taken from a human or an animal. The present invention is characterized by the feature that a dilution of the sample in the buffered aqueous extraction medium in a range of 1:100 to 1:10,000 is obtained. The present invention leads to a significant improvement of the technical situation, and provides a simple, sensitive and specific determination tool of proteins in GI tract samples. The determination of proteins, e.g. calprotectin, elastases or hemoglobin, in GI tract samples leads to more accurate and reproducible results.

A method of quantitatively determining the concentration of at least one analyte in a sample by: (i) adding a portion of the sample to a first analyte assay formulation and to an analyte assay reference formulation to generate a first analyte sample and analyte reference sample and determining the concentration of the at least one analyte in the sample and/or (ii) adding a portion of the sample to a second analyte assay formulation and determining the concentration of the at least one analyte in the sample, as well as formulations, kits of parts, systems and computer implemented methods associated with the method.

Methods, devices and systems for capturing biomarkers are provided. In particular, methods, compositions, and systems that utilize affinity capture devices comprising a processing chamber, affinity capture agent and porous membrane are provided.

The present invention relates to the field of affinity purification and provides for means and methods applying protein binding agents competing for a target protein for use as capture and elution tool, wherein the elution agent comprises an immunoglobulin single variable domain (ISVD), and is capable of displacing the capturing binding agent. More specifically, the displacement efficiency of the ISVD-containing protein binding agent is driven by its dissociation kinetics, with a rate constant of dissociation (k.sub.off) equal or lower as compared to the capturing agent. Furthermore, said protein binding agents are deployable in high-throughput purification from complex mixtures, or for capturing protein-complexes, thereby facilitating structural, biochemical and physicochemical analysis of said target proteins.

Analyzers and methods for making and using analyzers are described such as a method in which multiple absorption readings of a liquid assay are obtained by a photodetector using multiple light sources having at least three separate and independent wavelength ranges and with each of the absorption readings taken at a separate instant of time. Using at least one processor and calibration information of the liquid assay, an amount of at least two analytes within the liquid assay using the multiple absorption readings is determined.

Systems and methods are provided for sample processing. A device may be provided, capable of receiving the sample, and performing one or more of a sample preparation, sample assay, and detection step. The device may be capable of performing multiple assays. The device may comprise one or more modules that may be capable of performing one or more of a sample preparation, sample assay, and detection step. The device may be capable of performing the steps using a small volume of sample.

This present disclosure provides methods and compositions that can be used to quantify cfDNA in biofluids using a hybridization approach.

Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples. The values thus obtained are found to be valid indications of comparative total protein content, despite the fact that the tryptophan levels vary widely among the various proteins in any single sample and the samples, due to the diversity of their origins, tend to differ among themselves in the identities and relative amounts of the proteins that they contain. Protein samples are also normalized to correct for differences in sample dilution, sample loading, and protein transfer inconsistencies, by using stain-free detection of total protein in each of the samples, or detection of subsamples within each sample.

Provided is a reagent composition for measuring glycated albumin to diagnose the presence or absence of diabetes and a method of measuring glycated albumin using the same, and more particularly is a reagent composition for measuring glycated albumin, the composition including a dye-encapsulated silica nanoparticle-boronic acid, and to a method of measuring glycated albumin using the same. In the reagent composition for measuring glycated albumin, since a dye is encapsulated in silica nanoparticles, the inherent absorption wavelength of the dye is not affected by pH and the composition has excellent stability even when stored for one month or more.