Abstract: Described herein are monoclonal antibodies, assay kits and immumoassay methods for quantifying elastin fragments having a C-terminus amino acid sequence LPGGYGLPYT (SEQ ID NO: 1) in a patient biofluid sample, and uses thereof for detecting or quantifying fibrotic diseases such as chronic obstructive lung disease (COPD).

Abstract: The present invention relates to an assay for detecting Tumstatin, and its use in evaluating lung cancers, such as non-small cell lung cancer (NSCLC), chronic kidney disease (CKD), such as CKD resulting from diabetes, lupus nephritis (LN) and systemic lupus erythematosus (SLE).

Abstract: An antibody specifically reactive with an N-terminus neo-epitope of collagen type X alpha 1 comprised in the amino acid sequence H2N-GIATKGLNGP, and its use in an immunoassay for evaluating a disease associated with collagen type X alpha 1, such as osteoarthritis.

Abstract: An antibody specifically reactive with an epitope of collagen type X alpha 1 comprised in the NC1 domain C-terminal amino acid sequence SFSGFLVAPM-COOH (SEQ ID NO: 1), and a method of immunoassay for detecting in a biological sample an epitope in the NC1 domain C-terminal amino acid sequence SFSGFLVAPM-COOH (SEQ ID NO: 1) of collagen type X alpha 1, by contacting the biological sample with the antibody, and determining the amount of binding of the antibody.

Abstract: The present invention relates to an antibody, wherein the antibody specifically binds to the N-terminus of Lysyl Oxidase-Like 2 (LOXL2), and its use in a method of immunoassay for detecting or quantitating LOXL2 in a sample. The method may be used to evaluate LOXL2-associated diseases, and may also be used to evaluate the efficacy of anti-LOXL2 therapeutics.

Abstract: The present invention relates to an antibody, wherein the antibody is specifically reactive with short isoform collagen type XVIII, but does not react with intermediate isoform collagen type XVIII or with long isoform collagen type XVIII. The invention also relates to the use of the antibody in a method of immunoassay for detecting or quantitating short isoform collagen type XVIII, wherein the method may be used to evaluate haemophilic disease.

Abstract: The present invention provides an immunological binding partner reactive with a C-terminal epitope of the C5 domain of the ?3 chain of collagen Type 6, and a method of immunoassay using the immunological binding partner for detecting and quantifying the C-terminal epitope. The invention also provides a method of investigating the rate of formation of extracellular matrix and a method for identifying a subject suitable for treatment with an insulin sensitizer.

Abstract: Provided is a method of diagnosis or of quantitation of cancer. In the method a patient biofluid sample is obtained, an immunoassay is conducted to measure fragments of Nidogen-1 that have an N- or C-terminal neo-epitope formed by cleavage of Nidogen-1 by Cathepsin-S, where the fragments are naturally present in the sample, and associating an elevation of the measure in the patient above a normal level is associated with the presence or extent of cancer.

Abstract: A method of immunoassay for detecting in a biological sample a fragment of collagen type VII alpha 1 comprising an N- or C-terminal neo-epitope, the method comprising contacting the biological sample comprising the fragment of collagen type VII alpha 1 comprising the N- or C-terminal neo-epitope with an antibody of the invention, and determining the amount of binding of the antibody

Abstract: Provided is a method of bioassay for the quantification of N- or C-terminal neo-epitope biomarkers formed by cleavage of a CRP, ApoE, lumican, versican, perlecan, decorin, biglycan or elastin by a proteinase. The method includes contacting a biofluid sample with an antibody reactive with the neo-epitope biomarker and determining the level of binding of the antibody to the biomarker in the sample. The assay is predictive of risk of cardiovascular disease events.

Abstract: A method of bioassay for the quantification of peptide fragments elevated in lung diseases such as COPD, SCC, or IPF, comprising a neo-epitope formed at a cleavage site by cleavage in vivo of elastin by a proteinase by contacting a sample with an antibody having specific binding affinity for a the neo-epitope amino acid sequence and determining the level of binding, where the antibody binds one of the following terminal sequences: ...FGPGVV ...VPGLGV IKAPKL... and antibodies and immunoassay kits for use in such methods.

Abstract: The invention provides an immunological binding partner specifically reactive with a C-terminal epitope of the ?1 chain of collagen Type VIII or with an N-terminal epitope of the mature form of the ?1 chain of collagen Type VIII, and a method of immunoassay for detecting or quantitating in a sample the C-terminal epitope or the N-terminal epitope of the mature ?1 chain of collagen type VIII.

Abstract: Provided is a method of bioassay for the quantification of peptide fragments elevated in lung diseases such as COPD, SCC, or IPF. The peptide fragments comprise a neo-epitope formed at a cleavage site by cleavage in vivo of elastin by a proteinase. In the method a sample is contacted with an antibody having specific binding affinity for the neo-epitope amino acid sequence and determining the level of binding is determined where the antibody binds one of the following terminal sequences: . . . FGPGVV, . . . VPGLGV or IKAPKL . . . . Also provided are antibodies and immunoassay kits for use in such methods.

Abstract: The present invention provides an immunological binding partner reactive with a C-terminal epitope of the C5 domain of the ?3 chain of collagen Type 6, and a method of immunoassay using the immunological binding partner for detecting and quantifying the C-terminal epitope. The invention also provides a method of investigating the rate of formation of extracellular matrix and a method for identifying a subject suitable for treatment with an insulin sensitizer.

Abstract: A method of bioassay for the quantification of biomarkers useful in the diagnosis of fibrosis disease and prognosis of its development, including biomarkers indicative of the risk of developing fibrosis after a chronic injury is provided. In particular, according to the present invention, biomarkers relating to degradation fragments of Collagen type I, III, IV, V, and VI, elastin, C-reactive protein, and proteoglycans including Biglycan, Decorin, Versican, and Perlecan are found to be useful.

Abstract: Provided herein is a sandwich immunoassay for detecting cross-linked PIIINP that has at least two strands of PIIINP joined together by inter-strand cross-linking each having a C-terminal neo-epitope of PIIINP that is generated by N-protease cleavage of intact type III procollagen. A biological sample having the cross-linked PIIINP is contacted with a first surface-bound monoclonal antibody and then by a second monoclonal antibody, both specifically reactive with a neoepitope in the C-terminal sequence of PIIINP, and then binding of the second monoclonal antibody is determined. Also provided is a method for evaluating the efficacy of an antagonist drug targeting lysyl oxidases via the immunoassay and a kit containing a solid support binding the first monoclonal antibody and containing the second monoclonal antibody.

Abstract: Provided herein is a method of bioassay for the quantification of peptide fragments relevant to neurodegenerative conditions. The method comprises cleaving a Tau protein by a secretase, such as ADAM10, to form a neo-epitope. The method comprises contacting a blood derived sample with an antibody specific for the neo-epitope and determining the level of binding of the antibody to peptide fragments comprising the neo-epitope in the sample. Neo-epitope containing peptide levels are found to be inversely correlated to cognitive function.

Abstract: Provided is a monoclonal antibody specifically reactive with a C-terminal neo-epitope of PIIINP comprised in a C-terminal amino acid sequence CPTGXQNYSP-COOH (SEQ ID NO: 4) in which X is Gly or Pro, and where the monoclonal antibody does not recognize or bind an elongated version of the C-terminal amino acid sequence CPTGXQNYSPQZ-COOH (SEQ ID NO: 5), in which Z is absent or is one or more amino acids of the sequence of collagen type III. Also provided is a method of immunoassay for detecting in a biological sample the C-terminal neo-epitope of PIIINP generated by N-protease cleavage of intact type III procollagen, by contacting the sample with the monoclonal antibody, and determining the amount of binding of the antibody.

Abstract: Methods of diagnosis or of quantitation of fibrosis are provided that comprise conducting an immunoassay to measure neo-epitope containing protein fragments naturally present in a bioflui sample, and associating an elevation of the measure in the patient above a normal level with the presence or extent of fibrosis. The immunoassay is conducted by a contacting protein fragments naturally present in the sample with an immunological binding partner reactive with a neo-epitope formed by cleavage of a protein by a proteinase and measuring the extent of binding of peptide fragments to the immunological binding partner to measure therein protein fragments comprising the neo-epitope. The protein is collagen type I, collagen type IV, collagen type V, elastin, biglycan, decorin, lumican, versican, perlecan, neurocan, brevican, fibromodulin, serglycin, syndecan, betaglycan, vimentin, or C-reactive protein.

Abstract: Provided herein are methods of diagnosis or of quantitation of fibrosis. An immunoassay is conducted to measure neo-epitope containing protein fragments of collagen type III, collagen type I, collagen type IV, collagen type V, or collagen type VI, elastin, biglycan, decorin, lumican, versican, perlecan, neurocan, brevican, fibromodulin, serglycin, syndecan, betaglycan, vimentin, or C-reactive protein naturally present in a biofluid sample obtained from a patient. An above normal elevation of the measured protein fragments in the patient is associated with the presence or extent of fibrosis.