A method of determining protease activity in a biological sample comprising: (a) contacting the biological sample with a solution comprising a QZ probe to form a mixture; (b) incubating the mixture, thereby forming an incubated mixture comprising an incubated liquid; and (c) measuring the quantity of one or more analytes in a sample of the incubated liquid to determine the level of protease activity in the biological sample.

The present invention pertains to a new method for the diagnosis, prognosis, stratification and/or monitoring of a therapy, of cancer in a patient. The method is based on the determination of the level of a panel of biomarkers selected from CEA, AREG, IL-6, GDF-15, HGF-receptor, CXCL9, ErbB4-Her4, CXCLIO, Flt3L, VEGFR-2, CD69, CXCL5S, PSA, EMMPRIN, Cathepsin-D, Caspase-3, TNF-alpha, and INF-gamma. The new biomarker panel of the invention allows diagnosing and even stratifying various cancer diseases. Furthermore provided are diagnostic kits for performing the non-invasive methods of the invention.

The present disclosure provides methods in which adherent cells are treated with small molecules, cultured, lysed, and then analyzed by mass spectrometry to measure the activities of endogenous enzymes. The implementation of this method relies on the use of surfaces that are nanopatterned with cell adhesion ligands to mediate cell attachment and a peptide that is a substrate for the desired enzyme activity in the lysate.

Devices, bandages, kits and methods are described that can control or regulate the mechanical environment of a wound to ameliorate scar and/or keloid formation. The mechanical environment of a wound includes stress, strain, and any combination of stress and strain. The control of a wound's mechanical environment can be active, passive, dynamic, or static. The devices are configured to be removably secured to a skin surface in proximity to the wound site and shield the wound from endogenous and/or exogenous stress.

The invention relates to a novel chemical compounda diagnostic markerfor use in medicine, more specifically in cancer diagnosis, in particular the diagnosis of lung cancer. The invention also relates to an in vitro method for detecting enzymatic activity present in a subject's body fluid, in particular derived from lung cancer cells, using the compound. The invention further relates to an in vitro method for diagnosing lung cancer using the compound, a kit comprising the compound and use of the compound for the detection of enzymatic activity specific to lung cancer and use of the compound for the diagnosis of lung cancer. The invention also relates to the compound for use as a diagnostic marker of lung cancer and a method for the treatment of lung cancer comprising a step of carrying out the method for the diagnosis of lung cancer as defined above using the compound.

The present disclosure relates to methods of diagnosing lupus nephritis or proliferative lupus nephritis in a subject, methods of predicting a subject's risk of developing lupus nephritis and methods of determine whether a subject suffering from lupus nephritis is responding to treatment. The methods herein involve detecting the presence of or level of at least one biomarker which is IL-16, Galectin-1, CD163, CD206, FOLR2, proteinase 3, or a combination thereof.

Disclosed in the present invention is a method for detecting a protein having changes in an energy state, and affinity of a ligand to a protein. Specifically, after the energy state of a protein changes, its tolerance to proteolytic cleavage destruction changes. The structure of the protein in a low-energy state is also destroyed under a non-denaturation condition by using a large amount of enzymes, and small peptide fragments, which have molecular weight of less than 5 KDa and can be directly used for bottom-top mass spectrometry analysis, are directly generated. The method has extremely high sensitivity. Quantitative proteomics is used to find enzyme cleavage differential peptide fragments, and proteins to which the differential peptide fragments belong and the positions in the proteins are analyzed, so that a protein having changes in an energy state, and a change region can be determined in the whole proteome range. If the energy state of the protein changes due to addition of a ligand, the method can determine a binding protein and a binding region of the ligand; and the output of a quantitative result on the peptide fragment level further enables the method to determine the local affinity of binding of the ligand to the protein.

The present disclosure provides a method of identifying a substrate for a protease including contacting a protease to one of a first array and a second array, each array having the same plurality of features, each feature including at least one sequence linked to a solid support. The at least one sequence includes a candidate protease substrate linked to a reporter. The method further includes contacting a detectable element to each of the arrays to allow binding of the detectable element to the reporter, and detecting first and second signals resulting from binding of the detectable element to the each of the reporters in the first and second arrays. The method further includes comparing the first signal and the second signal to identify a difference in the first signal and the second signal, and identifying at least one candidate protease substrate as a substrate for the protease.

The present disclosure relates to library compositions, methods of making and screening libraries of peptidase-cleavable substrate sequences. In particular, the libraries are useful in identifying substrate sequences for a variety of disease- or tissue-specific peptidases. The present disclosure also relates to use of identified peptidase substrates to design therapeutic agents and diagnostic tools.

The present invention relates to materials and methods for high throughput monitoring of target engagement of isopeptidases, such as deubiquitylating enzymes by, inter alia, small molecule inhibitors. In particular the invention relates to development of high throughput assays to measure isopeptidase activity in biological samples, such as cells, animal tissues, animal tumours, human tissue or patient-derived biopsies.