A system of a recombinant bacteriophage library and a target of interest complex, wherein the recombinant bacteriophage peptide library includes a plurality of peptides expressed on the surface of recombinant bacteriophages wherein each recombinant bacteriophage includes (a) a pill protein; wherein each pill protein includes (b) a peptide or polypeptide involved in an intermolecular interaction, which differs by at least one amino acid from other peptides or polypeptides in the library; and (c) a modified protease cleavage site proximal to the peptide, wherein the modified protease cleavage site is the same in each bacteriophage, the modified cleavage site having a reduced binding affinity to a protease, as compared to a non-modified cleavage site, and wherein the target of interest complex includes a protease, a flexible linker attached to the protease, and a target of interest attached to the flexible linker, wherein the target of interest participates in an intermolecular interaction.

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.

This invention relates to the field of antibody quantification. In particular it relates to the quantification of antibodies in a biological sample; including anti-drug antibodies (ADA), anti-self antibodies (ASA), and mixtures thereof.

The invention relates generally to compositions and methods for detecting protease activity in a subject or a biological sample using activatable antibodies, and the use of these compositions and methods in a variety of diagnostic indications.

Assays for rapid measurement of total vitamin D in blood are provided. Vitamin D is measured following the rapid and irreversible release of vitamin D due to denaturation and digestion of vitamin D binding proteins by aspartyl peptidases (e.g., pepsin) under acidic conditions. Such measurements may be made using a vitamin D binder (e.g., an antibody) to measure competition between free vitamin D and added, labeled vitamin D. Synergy between denaturation and degradation is believed to provide more rapid and more complete release of vitamin D than would occur with acid or enzyme alone. These measurements may be made using small amounts of whole blood, serum, or plasma, and are suitable for use in automated devices. These methods provide the advantages of reduced cost, increased speed, reduced discomfort to the subject, and increased availability and ease of use. Reagents, kits, devices, and systems for these assays are also disclosed.

In one aspect, a homogenous assay method for determination of blood levels of legumain molecules (an asparaginyl endopeptidase) is disclosed. In one aspect, the assay utilizes specific sizes of nanoparticles that are coated with antibody or antibodies specifically towards legumain molecule or its fragment(s). In one aspect, the assay is designed in a homogenous manner with a dynamic range from 0.2 to 160 ng/mL. In another aspect, disclosed herein is a kit for assaying blood levels of legumain comprising two parts of reagents (R1 and R2), which kit is adaptable to be used on clinical chemistry analyzers. In one aspect, the cut-off values for differentiating normal from high risk of cancers such as breast cancer, colorectal cancer and stomach cancer are 183 ng/mL.

Some aspects of the present disclosure provide methods, compositions and kits for identifying one or more reagents, such as a culture medium, that are effective for recombinant protein production.

Novel synthetic catalytic structures or synzymes, e.g., synthetic polypeptides, with catalytic properties are provided. It is believed that these synthetic catalytic structures mimic some of the precise conformational changes necessary for catalytic activities seen in enzymes. The catalytic properties of these synthetic catalytic structures or synzymes can be further improved by the application of controlled external forces, e.g., electric fields.

An affinity reagent for analysing a biological sample includes a nucleic acid backbone, and a barcode oligonucleotide attached to the nucleic acid backbone. The nucleic acid backbone is configured to specifically bind to a target analyte by a complex structure thereof. The nucleic acid backbone is configured to maintain the complex structure in presence of the barcode oligonucleotide.

The invention relates to the field of biotechnology. The method for determining the spatial and temporal distribution of the activity of a proteolytic enzyme in an in vitro heterogeneous system, such as blood or blood plasma, involves the introduction of a luminescent, fluorogenic or chromogenic substrate into a sample with the subsequent release of a detectable tag as the proteolytic enzyme cleaves the substrate, and the recording of the optical characteristics of the sample, which makes it possible to assess the spatial and temporal distribution of the activity of the enzyme. The device for the implementation of the above method comprises an in vitro system, a means for illuminating the sample, a recording means and a control means. A method for diagnosing homeostatic imbalances according to a change in the spatial and temporal distribution of the activity of a proteolytic enzyme in a blood sample is also proposed.