Herein is reported a method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the steps of capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the first or the second antigen to form a captured antibody-antigen complex and determining a first binding signal, either i) incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal, or ii) regenerating the surface, capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the antigen not used for the formation of the captured antibody-antigen complex in step b) to form a captured antibody-antigen-antigen complex and determining a third binding signal, and determining the overall or individual binding of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal.

The invention relates to methods of reducing the immunogenicity of CRISPR-associated (Cas) proteins and the modified Cas proteins produced therefrom. In addition, the invention relates to methods for cell and gene therapy, including any and all genetic modifications and alterations of gene expression (and/or genetic elements) made in-vivo or ex-vivo using Cas proteins with reduced immunogenicity.

There are provided a method and a kit for evaluating allergen inactivators, the method and kit making it possible to carry out a precise and reproducible evaluation irrespective of the type of test drug, or the type of accompanying components thereof, that is subject to the evaluation.

A method for evaluating allergen inactivators, said method being characterized by comprising: a step for preparing an allergen-supporting membrane configured by supporting allergens on a membrane for supporting allergens; a step for treating the allergen-supporting membrane using a test drug; a step for washing the allergen-supporting membrane treated using the test drug, and subsequently treating the allergen-supporting membrane using antibodies specific to the allergens; a step for washing the allergen-supporting membrane treated using the antibodies specific to the allergens, and subsequently detecting the specific antibodies bound to the allergens; and a step for assessing the extent to which the allergens are inactivated by the test drug based on the detected quantity of the specific antibodies.

Provided herein, inter alia, are methods and compositions for identifying major histocompatibility class II (MEW II) complex binding peptides.

Disclosed are compositions and methods comprising the administration of pulsed dendritic cells and an immunoregulator molecule inhibitor for the treatment of cancer.

Ex vivo determination of increased tumor immunogenicity of a tumor biopsy is used as a guide to identify immunotherapy of a tumor in a patient. Most preferably, the ex vivo tests will include exposure of biopsy samples to stress conditions to produce pretreated tumor cells that are then assayed with immune competent cells for increased activation or activity. Test conditions include exposure of the biopsy samples to immune stimulatory compositions, antibodies against neoepitopes, and/or modified cells, and an increase of immunogenicity is preferably determined by their exposure to T cells and/or NK cells.

Provided is a novel high sensitive method for assaying misfolded SOD1 in a body fluid of a subject, in particular in the cerebrospinal fluid. This method is based on a novel highly sensitive immunoassay making use of a unique epitope of SOD1 and corresponding anti-SOD1 antibodies. In addition, kits comprising the components of the immunoassay are provided.

The present disclosure provides materials and methods for cell-free expression of epitopes for immunotherapy applications. In particular, the present disclosure provides materials and methods for expressing concatenated epitopes using a cell-free protein synthesis platform for high throughput, large scale, and unbiased epitope screening and the generation of multi-epitope vaccines.

The present invention provides for single-molecule profiling of combinatorial protein modifications and single-molecule profiling of combinatorial protein modifications combined with single-molecule sequencing of protein/nucleic acids complexes. High-throughput single-molecule imaging was applied to decode combinatorial modifications on millions of individual nucleosomes from pluripotent stem cells and lineage-committed cells. Applicants identified bivalent nucleosomes with concomitant repressive and activating marks, as well as other combinatorial modification states whose prevalence varies with developmental potency. Applying genetic and chemical perturbations of chromatin enzymes show a preferential affect on nucleosomes harboring specific modification states. The present invention also combines this proteomic platform with single-molecule DNA sequencing technology to simultaneously determine the modification states and genomic positions of individual nucleosomes. This novel single-molecule technology can be used to address fundamental questions in chromatin biology and epigenetic regulation leading to novel therapeutics and diagnostics.

Disclosed is a method of qualifying a subgroup of target binding biomolecules from a larger group of target binding biomolecules for analysis. A competitive immunoassay including a target protein is used to identify 100 interactions between different pairs of the target binding biomolecules and interaction profiles are generated 200. Each target binding biomolecule is allocated 300 to a bin representing an epitope family and identified bins are associated in a circular or semi-circular bin chart on a display with identified respective target binding biomolecule(s). Based on the association 400 between identified bins and identified respective target binding molecule(s) in the bin chart, a subgroup of target binding biomolecules is selected 500 for further analysis by selecting one or more of the target binding biomolecule(s) of one or more of the bins.