The present application provides methods and systems to identify host cell protein (HCP) impurities in a sample containing high-abundance proteins. The HCP impurities can be enriched using interacting peptide ligands which have been attached to solid support. The HCP impurities can be eluted from the solid support using solution containing phase transfer surfactants. The isolated HCP impurities can be digested to generate components of the isolated HCP impurities which can subsequently be identified using a mass spectrometer.

Multiplexed test measurements are conducted using an assay module having a plurality of assay domains. In preferred embodiments, these measurements are conducted in assay modules having integrated electrodes with a reader apparatus adapted to receive assay modules, induce luminescence, preferably electrode induced luminescence, in the wells or assay regions of the assay modules and measure the induced luminescence.

The present invention provides assays and assay systems for use in spatially encoded biological assays. The invention provides an assay system comprising an assay capable of high levels of multiplexing where reagents are provided to a biological sample in defined spatial patterns; instrumentation capable of controlled delivery of reagents according to the spatial patterns; and a decoding scheme providing a readout that is digital in nature.

The invention relates to devices and methods for the detection of specific interactions between probe and target molecules. In particular, the invention relates to methods for the qualitative and/or quantitative detection of targets, including: introducing a sample containing targets into a reaction chamber formed between a first surface of the device and a second surface of a device, which is preferably located opposite to the first surface, wherein the distance between the first and the second surface is variable; and detecting the targets.

A peptide that binds specifically to neuropilin-1 (NRP1) without binding to neuropilin-2 (NRP2) is provided. A fusion protein, a fusion antibody, small-molecule drug, a nanoparticle, or a liposome, which comprises the peptide, and a pharmaceutical composition for treating or preventing cancer or angiogenesis-related diseases, and a composition for diagnosing cancer or angiogenesis-related diseases are provided. A polynucleotide encoding the peptide that binds specifically to NRP1 and a method for screening the peptide that binds specifically to NRP1 are provided. An antibody heavy-chain constant region Fc-fused peptide binding specifically to NRP1 has the property of binding specifically to NRP1, and thus when it is administered in vivo, it accumulates selectively in tumor tissue, and widens the intercellular space between tumor-associated endothelial cells to promote its extravasation and increases its tumor tissue penetration.

Contemplated test kits and methods for food sensitivity are based on rational-based selection of food preparations with established discriminatory p-value. Particularly preferred kits include those with a minimum number of food preparations that have an average discriminatory p-value of ≤0.07 as determined by their raw p-value or an average discriminatory p-value of ≤0.10 as determined by FDR multiplicity adjusted p-value. In further contemplated aspects, compositions and methods for food sensitivity are also stratified by gender to further enhance predictive value.

The present invention relates to inhibitors of HIF-1 and HIF-2 and uses thereof. The present invention further relates to the inhibitors for use in treatment of diseases. An isolated polypeptide is provided, that prevents dimerization of HIF-1α with HIF-1β and HIF-2α with HIF-1β and/or inhibits the activity of HIF-1 and HIF-2, wherein the polypeptide comprises the amino acid sequence C-X1-X2-X3-Z-X4 (SEQ ID NO: 1) and wherein X1, X2, X3 and X4 are any amino acid and wherein Z is leucine, valine of isoleucine or a non-natural derivative or leucine, valine or isoleucine. The isolated polypeptide prevents dimerization of HIF-1α with HIF-1β and HIF-2α with HIF-1β and inhibits the activity of HIF-1 and HIF-2 by binding to HIF-1α or HIF-1β and/or HIF-2α or HIF-1β.

Compositions and methods for detecting molecule-molecule interactions are provided. The methods employ a prokaryotic ubiquitin-like protein (Pup) and a Pup ligase that is coupled to one of the molecules. When the Pup ligase is brought to proximity to the other molecule by virtue of the molecule-molecule interaction, the Pup ligase can conjugate the Pup to a lysine residue on the other molecule. As such conjugation can be easily detected, this method allows easy identification of the molecule-molecule interaction.

Compositions and methods for displaying antibodies in the periplasmic space of yeast cells are disclosed. In particular, antibodies are linked to a cell membrane-spanning transmembrane domain, a cell-membrane associated protein domain that is on the external face of the yeast cell membrane, a protein that binds to the inner face of the yeast cell wall, or a periplasmic protein in order to display the antibodies in the yeast periplasmic space. In addition, a target protein of interest can be coexpressed in yeast such that it is localized to the plasma membrane or periplasmic space and accessible to binding by displayed antibodies. The disclosure further relates to high-throughput screening of antibody libraries using yeast cell periplasmic display.

The invention relates generally to synthetic non-antibody protein scaffolds (synNAPS) that differentially detect or quantitate a target insecticidal protein in a complex biological matrix comprising the target protein and a non-target insecticidal protein and to methods of using the synNAPS in immunoassays, and more particularly to monoclonal antibodies and immunoassays for the differential detection and quantitation of a wild-type crystal protein, such as a wild-type-Cry1Ab, from Bacillus thuringiensis and hybrid crystal proteins, which comprise all or a significant portion of the wild-type Cry protein in complex biological samples comprising both the wild-type Cry protein and one or more of the hybrid Cry proteins.