Abstract: Disclosed herein are methods, kits, and systems for detecting or determining an amount, quantity, concentration and/or level of immunoglobulin G, subclass 4 (LgG4) in a biological sample from a subject. Particularly, the methods, kits and systems are directed to detection of IgG4 using an anti-IgG4 antibody that does not cross-react with other IgG subclasses.

Abstract: This disclosure provides a robust, sensitive, and specific assay for the detection and measurement of periostin levels in samples obtained from human patients having, or suspected of having an IL-13-mediated disease or disorder. The disclosure further provides novel antiperiostin monoclonal antibodies that recognize at least isoforms 1, 2, 3, 4, 7, and 8 of human periostin, and assay kits comprising one or more of these antibodies.

Abstract: This disclosure provides a robust, sensitive, and specific assay for the detection and measurement of periostin levels in samples obtained from human patients having, or suspected of having an IL-13-mediated disease or disorder. The disclosure further provides novel antiperiostin monoclonal antibodies that recognize at least isoforms 1, 2, 3, 4, 7, and 8 of human periostin, and assay kits comprising one or more of these antibodies.

Abstract: Provided herein are antibodies and methods of using the antibodies to treat, prevent, modulate, attenuate and diagnose iron-related disorders.

Abstract: The present invention relates to antibodies that immunospecifically bind to human brain natriuretic peptide or a human brain natriuretic peptide fragment with a high binding affinity, methods for producing and selecting said antibodies, immunoassays for human brain natriuretic peptide or a human brain natriuretic peptide fragment that employ said antibodies and therapeutic compositions containing said antibodies.

Abstract: The present invention relates to antibodies that specifically bind to human BNP and immunoassays using said antibodies in the quantification of human BNP or a fragment of human BNP in a test sample.

Abstract: Provided herein are combinatorial libraries containing chimeric Major Histocompatibility Comples (MHC) Class I proteins displayed on the surfaces of recombinant yeast cells. Members of the libraries, especially where those libraries have been mutagenized either with error-prone Polymerase Chain Reaction or with site-directed oligonucleotide mutagenesis, are improved in conformation stability or in binding to a target, e.g., a peptide or other ligand as compared with the stability or binding affinity of a wild type MHC Class I chimeric protein. The improved mutant chimeric proteins can be selected by various means, including fluorescence activated cell sorting with a fluorescent ligand bound to the surfaces of the yeast cells displaying the improved mutant chimeric protein.