This invention discloses diagnosis of risk of chemotherapy-induced cardiotoxicity by measurement of increased expression of soluble epoxide hydrolase in vitro and in vivo in cells, tissues or animals including measurement of increased levels of soluble epoxide hydrolase metabolites, e.g., 14,15-DHET and 11,12-DHET, in biological fluids. This invention also includes diagnosis of risk of chemotherapy-induced cardiotoxicity by measuring increased levels of oxidative stress in cells, tissues or animals including measurement of increased levels of oxidative stress biomarkers, e.g., 8-isoprostane, in biological fluids. Fatty acid and protein biomarkers to diagnose the risk of chemotherapy-induced cardiotoxicity are detected using various detection methods including mass spectrometry and immunoassay such as ELISA, Western blot analysis or label-free microwell and nanowell technologies. This invention discloses targeted medical intervention for a subject who is at risk or with chemotherapy-induced cardiotoxicity by treating with soluble epoxide hydrolase inhibitor(s) with or without antioxidants to prevent or ameliorate the chemotherapy-induced cardiotoxicity.

Provided are methods for identifying OP-adducted biomarkers of OP exposure as well as compounds containing OPs that can provide OP adducts and compounds of Formula 1 for eliciting antibodies that specifically and selectively bind to the OP adducts, wherein the Formula 1 compounds have the structure of OP-Peptide-Linker-CP, wherein CP is a carrier protein, OP represents a structure corresponding to that of a reactive organic phosphorous compound covalently modifying a tyrosine residue hydroxyl group of the peptide of Formula I and the other variable groups are as described herein.

Provided herein are methods, compositions and articles of manufacture for use in connection with cell therapy involving the administration of one or more doses of a therapeutic T cell composition. The cells of the T cell composition express recombinant receptors such as chimeric receptors, e.g. chimeric antigen receptors (CARs) or other transgenic receptors such as T cell receptors (TCRs). Features of the provided embodiments, including the numbers of cells or units of cells administered and/or the potency of administered cells, provide various advantages, such as lower risk of toxicity in subjects administered the T cell compositions.

Processes and compositions for the therapeutic treatment of pathogenic Gram-negative bacterial infection are provided whereby argininosuccinate synthetase or PEGylated argininosuccinate synthetase is administered to a subject to inactivate endotoxin thereby reducing the likelihood of bacterial sepsis and improving patient outcome.

A method for determining past exposure to chemical agents or heavy metals may include coating a capture material with a capture reagent. The capture reagent may be selected based on an ability of the capture reagent to bind with a target antibody, and the target antibody may be an indicator associated with a particular chemical agent or heavy metal. The method may further include interrogating a clinical sample associated with an individual by forming a mixture of the capture material and the clinical sample, and determining an exposure status of the individual to the particular chemical agent or heavy metal based on whether the capture material demonstrates capture of the indicator.

Anaplasma phagocytophilum surface proteins Asp14 and OmpA and homologous genes from Anaplasmatacaea family members are used in compositions suitable for vaccines to treat or prevent infections caused by tick-born bacteria of the Anaplasmatacaea family. Asp14 and/or OmpA proteins or peptide fragments may be used in combination with other Anaplasmatacaea surface proteins to elicit an immune response. Furthermore, antibodies to Asp14 and/or OmpA proteins can be used in diagnostic methods to determine whether an individual has contracted an Anaplasmatacaea infection. Because of the conserved invasin domains in the surface proteins, a wide range of Anaplasmatacaea infections may be diagnosed, treated or prevented using compositions of the invention.

A method for determining past exposure to chemical agents or heavy metals may include coating a capture material with a capture reagent. The capture reagent may be selected based on an ability of the capture reagent to bind with a target antibody, and the target antibody may be an indicator associated with a particular chemical agent or heavy metal. The method may further include interrogating a clinical sample associated with an individual by forming a mixture of the capture material and the clinical sample, and determining an exposure status of the individual to the particular chemical agent or heavy metal based on whether the capture material demonstrates capture of the indicator.

Anaplasma Marginale surface protein OmpA and homologous genes from Anaplasmatacaea family members are used in compositions suitable for vaccines to treat or prevent infections caused by tick-born bacteria of the Anaplasmatacaea family. OmpA proteins or peptide fragments may be used in combination with other Anaplasmatacaea surface proteins to elicit an immune response. Furthermore, antibodies to OmpA proteins can be used in diagnostic methods to determine whether an individual has contracted an Anaplasmatacaea infection.

The present invention provides an oxygenated fatty acyl glycerol for use in treating and/or preventing an inflammatory disease a subject.

A sample analysis device used to detect a level of exposure of organophosphorus within a sample comprising a sample collection pad, at least one conjugate zone comprising an anti-analyte antibody that is conjugated with a reporter label, and a control antibody that is conjugated with a reporter label, a blocking and/or test zone comprising an immobilized nanoparticle or other molecule that captures the Organophosphate-bound analyte, a second blocking and/or test zone comprising an immobilized antibody that binds to the unbound analyte and an optional third blocking and/or control zone comprising an immobilized antibody that binds to the control molecule wherein, when the analyte is bound by the Organophosphate in the sample it will bind to the first test line, and if the analyte is free from the Organophosphate it will bind to the second test line, and the control antibody will bind to the control line.