A method of analyzing protein-protein interactions includes binding the first proteins to the substrate where the first proteins are tagged with the first markers which bind specifically to the biomolecules immobilized on the substrate or the first proteins bind specifically to the biomolecules immobilized on the substrate; incubating the substrate bound first proteins with cell lysate containing the second proteins which are tagged with second markers; analyzing the interactions between the first proteins and the second proteins in the cell lysate, and obtaining the first analytic value representing the kinetic picture of the interactions; incubating the substrate bound first proteins with cell lysate mixture of a cell lysate consisting of the second markers-tagged second proteins and another cell lysate comprising other proteins including unlabelled second proteins and obtaining the second analytic value; comparing and analyzing the first and the second analytic values.

Antibody-based methods of detecting of molecules interacting with a target molecule, such as a nuclear or cytoplasmic protein, in a fixed and, optionally, permeabilized cell or tissue sample. In one example, the target molecule is bound by a primary antibody, and a secondary, peroxidase-conjugated antibody, then binds to the primary antibody. The peroxidase may also be conjugated the primary antibody. Biotin tyramide is added to the sample, and the peroxidase generates short-lived intermediates resulting in biotinylation of molecules adjacent to the peroxidase. Biotinylated molecules can be isolated from the sample by affinity interaction with avidin- or streptavidin, resulting in a fraction containing biotinylated molecules that are located in the sample in proximity to the target molecule. The fraction can be analyzed by mass-spectroscopy, Western blotting, sequencing and other techniques.

The invention relates generally to polypeptides, such as antibody molecules, that demonstrate high stability and solubility. In particular, the invention relates to polypeptides comprising paired V.sub.L and V.sub.H domains that demonstrate soluble expression and folding in a reducing or intracellular environment. The invention also relates to polynucleotides encoding such polypeptides, to libraries of such polypeptides or polynucleotides, and to methods of using such polypeptides in research, diagnostic and therapeutic applications.

A method for the quantitative characterization of amyloid and/or aggregated peptides and/or proteins in a sample, comprising:providing a sample, wherein the sample includes an amyloid and/or aggregated peptide and/or protein having at least one aggregate size and shape;adding an active ingredient to be analyzed to the sample solution;separating the amyloid and/or aggregated peptides and/or proteins are from one another according to their aggregate size and shape;optionally completely denaturing the amyloid and/or aggregated peptides and/or proteins of a particular fraction into monomer building blocks;determining the change in concentration of the peptide and/or protein building blocks in at least one fraction by comparison against control values without the active ingredient.

Microfluidic devices for determining whether an analyte is present in a sample are provided. The microfluidic devices include a polymeric medium that includes a first analyte detection domain having a first covalently bound capture member that specifically binds to a first analyte, and a second analyte detection domain having a second covalently bound capture member that specifically binds to a second analyte. Also provided are methods of using the subject microfluidic device, systems and kits that use the subject microfluidic devices, as well as methods of producing the same.

A method for cell-free protein synthesis is characterized in that pH is controlled by using an enzyme. For example, by using an amino acid decarboxylase, the pH is controlled according to removal of hydrogen ions that are produced during regeneration of ATP. The method for cell-free protein synthesis of the present invention has an advantage that not only the expression amount of protein is enhanced but also the expressed protein can be directly used for activity analysis without undergoing any separation or purification.

Provided are dyes and compositions which are useful in a number of applications, such as the detection and monitoring protein aggregation, kinetic studies of protein aggregation, neurofibrillary plaques analysis, evaluation of protein formulation stability, and analysis of molecular chaperone activity.

The present application provides arrays for use in immunosignaturing and quality control of such arrays. Also disclosed are peptide arrays and uses thereof for diagnostics, therapeutics and research.

According to an example aspect of the present invention, there is provided a method for determining the presence of a biomarker for disease in a pretreated biological sample comprising the steps of diluting the sample, contacting the sample with a europium label, a terbium label or a samarium label, and a dye, contacting the sample with a phage, incubating the sample, measuring luminescence emission intensity or absorption emission intensity, and determining the presence of the biomarker based on the measurement of the luminescence emission intensity or the absorption emission intensity.

A method for discriminating between Parkinson's disease and multiple system atrophy, the method comprising the steps of: (1) preparing a solution containing ?-synuclein monomers having a tendency to produce rod-like aggregates and/or a solution containing ?-synuclein monomers having a tendency to produce twisted aggregates; (2) adding a biological sample from a subject to the solution(s) containing the ?-synuclein monomers prepared in step (1); (3) allowing the ?-synuclein monomers to aggregate in the solution(s) obtained in step (2); and (4) detecting ?-synuclein aggregates formed in step (3).