This disclosure relates generally to novel kits for measuring insect health, and to methods of making and using such compositions. More specifically, the invention relates to novel kits for a rapid and high-throughput measurement of lipase activity levels in insects, and the correlation of the measured lipase activity levels with insect stress.

Provided herein are methods for modulating follistatin, such as inhibiting follistatin, suppressing the production of follistatin, reducing the level of follistatin, inhibiting the function of follistatin, or a combination thereof. The method can include administration of a compound that acts to modulate follistatin. In one embodiment, the compound is administered to a patient having or at risk or having a disease or condition selected from diabetes, pre-diabetes, metabolic syndrome, insulin resistance, dementia, and obesity, and optionally the disease or condition is prevented, treated, ameliorated, or a combination thereof.

An object of the present invention is to provide a highly versatile, simple and safe method for measuring Lp-PLA.sub.2 activity. Another object of the present invention is to provide an accurate and highly sensitive method for measuring Lp-PLA.sub.2 activity. Provided is a method for measuring lipoprotein-associated phospholipase A.sub.2 (Lp-PLA.sub.2) activity in a sample containing Lp-PLA.sub.2, the method comprising the following steps (A) to (C): (A) converting PAFs into lyso-PAFs by reacting the PAFs with the Lp-PLA.sub.2 in the sample; (B) hydrolyzing the lyso-PAFs produced in the step (A) with an enzyme (lyso-PAF-PLD) to obtain hydrolysate; and (C) measuring Lp-PLA.sub.2 activity in the sample by utilizing a quantitative change attributable to the hydrolysate obtained in step (B) as an indicator.

A biosensor for detecting a biomarker in a bodily fluid, secretion or exudation is described that includes a first electrode, a second electrode, an electrode coating and a mechanical electrode stabilizer. The biomarker is an enzyme catalyzing a chemical reaction in which a singularity or plurality of constituents of the electrode coating are chemically altered by the breaking of covalent chemical bonds when being in contact with the same. The electrode coating can be a natural or synthetic substrate of the biomarker. The first electrode and the second electrode are electrically conductive and are kept in a substantially constant and uniform distance from each other by means of the mechanical electrode stabilizer. The exposed electrically conductive surface of at least one of the first electrode and the second electrode are substantially fully covered by the electrode coating.

Provided is a compound having the structure:

(SIG)-(SI-MOD).sub.m

where SIG is a signaling molecule, SI is a self-immolative structure bound to SIG such that SIG has a reduced signal relative to the signal of SIG without SI, MOD is a moiety bound to SI that is subject to modification by an activator, and m is an integer from 1 to about 10. When MOD is modified by an activator, SI is destabilized and self-cleaved from SIG such that SIG generates an increased signal. Also provided are methods of determining whether a sample, such as a cell, comprises an activator, such as a nitroreducase, using the compound. Further provided are methods of determining whether a mammalian cell is hypoxic using the compound where nitroreductase is the activator. A method of detecting a microorganism that comprises a nitroreductase using the compound where nitroreductase is the activator is also provided.

Provided is a compound having the structure:
(SIG)-(SI-MOD).sub.m
where SIG is a signaling molecule, SI is a self-immolative structure bound to SIG such that SIG has a reduced signal relative to the signal of SIG without SI, MOD is a moiety bound to SI that is subject to modification by an activator, and m is an integer from 1 to about 10. When MOD is modified by an activator, SI is destabilized and self-cleaved from SIG such that SIG generates an increased signal. Also provided are methods of determining whether a sample, such as a cell, comprises an activator, such as a nitroreducase, using the compound. Further provided are methods of determining whether a mammalian cell is hypoxic using the compound where nitroreductase is the activator. A method of detecting a microorganism that comprises a nitroreductase using the compound where nitroreductase is the activator is also provided.

Lysosomal acid lipase (LAL) substrates, assays for lysosomal acid lipase using the substrates, and methods for diagnosing diseases and conditions attributable to lysosomal acid lipase deficiency.

The present invention is related to a method for evaluation of drug efficacy of a medicine having a therapeutic or preventive effect against a disease related to EL activity wherein phosphatidylinositol or lysophosphatidylinositol is used as an indicator. The present invention is also related to a method for screening an inhibitor of EL activity using phosphatidylinositol and a kit for use in the method.

Reagents, assays, methods, kits, devices, and systems for rapid measurement of cholesterol and cholesterol sub-fractions from a blood sample are provided. Total cholesterol, low density lipoprotein cholesterol, and high density lipoprotein cholesterol can be measured in a single assay using kinetic measurements, under conditions in which cholesterol sub-species are converted to a detectable product at distinct rates. The detectable product is measured at different times after assay initiation. A lipase, cholesterol esterase, cholesterol oxidase and a peroxidase may be used together to produce colored product in amounts directly proportional to the quantity of cholesterol converted. Methods for calculating very-low density lipoprotein cholesterol levels by further including triglyceride measurements are disclosed. Assays may be performed in a single reaction mixture, allowing more accurate and precise cholesterol determinations, including ratios of cholesterol sub-fractions to total cholesterol, at less expense, than would be expected by performing several different assays in different reaction mixtures.

An object of the present invention is to provide a highly versatile, simple and safe method for measuring Lp-PLA.sub.2 activity. Another object of the present invention is to provide an accurate and highly sensitive method for measuring Lp-PLA.sub.2 activity. Provided is a method for measuring lipoprotein-associated phospholipase A.sub.2 (Lp-PLA.sub.2) activity in a sample containing Lp-PLA.sub.2, the method comprising the following steps (A) to (C): (A) converting PAFs into lyso-PAFs by reacting the PAFs with the Lp-PLA.sub.2 in the sample; (B) hydrolyzing the lyso-PAFs produced in the step (A) with an enzyme (lyso-PAF-PLD) to obtain hydrolysate; and (C) measuring Lp-PLA.sub.2 activity in the sample by utilizing a quantitative change attributable to the hydrolysate obtained in step (B) as an indicator.