Proteases regulate a wide range of normal cellular functions where dysregulated activity is observed in various diseases. Compositions and methods use protease activity multiplexed bead-based immunoassays to profile protease activity. This platform technology integrates protease activity measurements with total protein quantification techniques. It represents a significant improvement over existing detection techniques by allowing for multiplexed, sensitive active protease measurements in complex biological samples. Exemplary multiplexed detections are realized in a single assay using a minute sample amount (e.g., 5 l) for active recombinant MMP-1, -2, -3, -7, 9, and 12 and those same MMPs in cell culture supernatant, menstrual fluid effluent, and peritoneal aspirates. This multiplexed platform achieves high level of sensitivities equal to or better than existing leading single-plex detection strategies. It also allows for high throughput screening to identify inhibitors of proteases in complex, donor-derived samples.

The present invention relates to a method for quantifying a therapeutic antibody in a sample of a human individual comprising a step of adding to a test sample which may contain therapeutic antibodies to be quantified a known amount of two or more labeled forms of said therapeutic antibodies.

The disclosure provides constructs comprising a first fusion protein, a second fusion protein, and a linker, wherein the first fusion protein and the second fusion protein each include an affinity reagent and a reactive enzyme, and the linker includes a first and second functional groups specific for irreversibly inhibiting the first and second fusion protein reactive enzymes. The disclosure further provides a method including (a) contacting a first fusion protein including an affinity reagent and a reactive enzyme with a linker including a functional group specific for irreversibly inhibiting the first fusion protein reactive enzyme thereby coupling the first fusion protein and the linker, and (b) contacting a second fusion protein including an affinity reagent and a reactive enzyme with the linker, the linker including a functional group specific for irreversibly inhibiting the second fusion protein reactive enzyme thereby coupling the second fusion protein and the linker.

The present invention provides a sufficiently effective medicine for treatment and/or prevention of ischemic diseases, without performing isolation of therapeutic cells or removal of deleterious cells from blood cells/hemocytes. The blood cells and/or the hemocytes are subjected to the action of a saccharide. The saccharide is a monosaccharide, a disaccharide, a trisaccharide, a polysaccharides, or a copolymer containing a monosaccharide, a disaccharide, or a trisaccharide as a component. The saccharide is a copolymer of sucrose and epichlorohydrin.

Disclosed herein is a composition comprising a crosslinked hydrogel; where the hydrogel comprises a polymer having a cleavable bond along a backbone of the polymer, along a substituent that undergoes crosslinking, or along the backbone of the polymer and along the substituent that undergoes crosslinking; where the cleavable bond is operative to be cleaved by an enzyme released in the body of a living being; and a semiconducting quantum dot that emits light in the visible portion of the electromagnetic spectrum.

A transgenic non-human mammal has a genome that includes an early-immediate enhancer of human cytomegalovirus (CMV enhancer), a -actin promoter and the entire gene region of human matrix metalloproteinase 2 (hMMP2) disposed downstream of the promoter. The hMMP2 is systemically expressed in the transgenic non-human mammal, which thus provides a suitable animal model for studying chronic obstructive pulmonary disease and related diseases and conditions.

Provided are peptides, and conjugates comprising targeting peptides and payloads. The peptides comprise a plurality of modules corresponding to at least one of module 1, module 2, or module 3 of the collagen binding domain of a gelatinase, or a gelatin-binding fragment or variant thereof. The gelatinase may be MMP-2. The conjugates may be therapeutic or non-therapeutic. Medical uses of the peptides or therapeutic conjugates, and pharmaceutical compositions comprising these, are also provided, as are nucleic acids encoding the peptides.

The invention relates to an enzyme solution, which is used preferably for pre-treating mammalian cells for flow-cytometric detection of light chain restriction of the cells, the enzyme solution comprising at least two proteases, which are proteolytic and also collagenolytic, in a buffer. Preferably, the enzyme solution comprises trypsin, collagenase 4, dispase and astacin. The invention also relates to uses of the enzyme solution and methods for flow-cytometric detection of light chain restriction of cells.

Disclosed are pharmaceutical compositions and methods for digesting atherosclerotic plaques in a patient in need thereof. The compositions include and the methods utilize a mixture of collagenases for digesting plaques and optionally may include or utilize additional agents such as cyclodextrins, chelating agents, and tissue plasminogen activator.

The disclosure provides constructs comprising a first fusion protein, a second fusion protein, and a linker, wherein the first fusion protein and the second fusion protein each include an affinity reagent and a reactive enzyme, and the linker includes a first and second functional groups specific for irreversibly inhibiting the first and second fusion protein reactive enzymes. The disclosure further provides a method including (a) contacting a first fusion protein including an affinity reagent and a reactive enzyme with a linker including a functional group specific for irreversibly inhibiting the first fusion protein reactive enzyme thereby coupling the first fusion protein and the linker, and (b) contacting a second fusion protein including an affinity reagent and a reactive enzyme with the linker, the linker including a functional group specific for irreversibly inhibiting the second fusion protein reactive enzyme thereby coupling the second fusion protein and the linker.