Methods for producing high concentration protein formulations having high stability are provided. Assays for selecting proteins and formulation conditions that have high self-repulsive attributes are used as an early step in the manufacturing process. Specifically, a protein concentration-dependent self-interaction nanoparticle spectroscopy method is employed as a protein colloidal interaction assay.

The present invention relates to devices, kits, instruments and methods for quantitatively detecting multiple analytes in a sample. More specifically, the present invention relates to devices, kits, instruments and methods for quantitatively detecting multiple analytes with desired or targeted precision, and the uses thereof.

The present invention relates to a method for detecting a spatial proximity of a first and a second epitope (11, 21) of a protein or of a first and a second protein (10, 20) of a protein complex (1) in a sample of a subject. The method comprises binding a first binding member (30) having a first oligonucleotide (31) conjugated thereto to the first epitope (11), binding a second binding member (40) having a second oligonucleotide (41) conjugated thereto to the second epitope (21), and determining whether a Fluorescence Resonance Energy Transfer (FRET) effect is present between a donor fluorophore (32) and an acceptor fluorophore (42), which are associated with the first oligonucleotide (31) and the second oligonucleotide (41), wherein the presence of the FRET effect indicates a spatial proximity of the first and the second oligonucleotide (31, 41) and, thus, the spatial proximity of the first and the second epitope (11, 21).

An IROA Matrix of metabolite compounds is disclosed. Each of whose compounds has a molecular weight of 2000 AMU or less, and is present as first and second isotopomers that are equally present at two predetermined isotopomeric balances, and contain 2 to 10% of a first isotope, and 90 to 98% of a second isotope, respectively. A reagent pair for transforming a natural abundance mass spectral analysis metabolite sample into an IROA sample is also disclosed and comprises two reactively identical reagents that constitute first and second isotopomers containing 2 to 10% of a first isotope, and 90 to 98% of a second isotope, respectively. Each of the reagent pair contains the same reactive group that reacts with and bonds to a functional group of one or more compounds present in a composition of biologically-produced metabolite compounds. Methods of making and using the above and related materials are also disclosed.

The present disclosure provides a method of identifying a peptide antigen, including contacting an antibody-comprising composition to a peptide microarray having an array surface and a plurality of feature pairs disposed thereon. Each of the feature pairs includes a first feature of wild-type peptides having a defined sequence and a second feature of mutant peptides having the defined sequence with a single amino acid mutation. Each of the wild-type peptides and the mutant peptides has an array-coupled terminus coupled to the array surface and an opposing free terminus, and the position of the amino acid mutation in the mutant peptides is located closer to the array-coupled terminus of the mutant peptides than the free terminus. The method further includes detecting binding of an antibody in the antibody-comprising composition to at least one of the feature pairs on the peptide microarray, and identifying feature pairs exhibiting differential binding.

In one aspect, compositions and methods are described herein for providing a microenvironment mapping platform operable to selectively identify various features, including protein-protein interactions on cellular membranes. In some embodiments, a composition comprises a catalyst, and a protein labeling agent, wherein the catalyst activates the protein labeling agent to a reactive intermediate. The catalyst, in some embodiments, can have electronic structure for permitting energy transfer to the protein labeling agent to form the reactive intermediate. The reactive intermediate reacts or crosslinks with a protein or other biomolecule within the diffusion radius of the reactive intermediate.

Provided herein are cell assay devices, methods of assaying the activity of immune cells on target cells, and methods of selecting a treatment for a subject having cancer. Described herein are cell assay devices comprising a biocompatible substrate having an upper surface supporting a plurality of arrays of spots comprising an adhesion-promoting material; a biocompatible membrane having top and bottom surfaces and positioned adjacent to the upper surface of the substrate and defining a plurality of chambers within the membrane between the top surface and the bottom surface of the membrane, wherein the membrane comprises at least two openings in the top surface of the membrane into each chamber to provide access to the chambers.

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.

A method is described for identifying high affinity monoclonal antibody heavy and light chain pairs from high throughput screens of antibody producing cell libraries such as B-cell and hybridoma libraries. Specifically, the method relates to application of reversed immunocapture and high resolution tandem mass spectrometry for the identification of heavy and light chain pairs of binding antibodies obtained from high throughput screens of antibody producing cell libraries.

The disclosure relates to a virus-like particle in which a protein complex is entrapped, ensuring the formation of the protein complex under physiological conditions, while protecting the protein complex during purification and identification. The disclosure further relates to the use of such virus-like particle for the isolation and identification of protein complexes.