Abstract: A method of manufacturing a metal fabric or membrane, the method comprises providing an ink comprising a plurality of semiconductor particles disposed in a first solvent. The method comprises applying the ink to a fabric or membrane to obtain a fabric or membrane comprising a plurality of semiconductor particles. Finally, the method comprises contacting the fabric or membrane comprising the plurality of semiconductor particles with a deposition solution comprising a second solvent, an autocatalytic agent, and metal cations to thereby cause a reaction to occur such that the metal cations are reduced and at least partially displace the semiconductor particles, to thereby provide a metal fabric or membrane.

Abstract: Systems, methods, and test kits for detecting and quantifying an analyte level in a biological fluid sample using impedance measurements, are disclosed. The fluid sample is applied to a lateral flow strip, and impedance of the strip is measured as the assay dries. Analysis of the drying-dependent impedance measurements indicates the presence and quantity of the analyte in the fluid sample.

Abstract: Systems, methods, and test kits for detecting and quantifying an analyte level in a biological fluid sample using impedance measurements, are disclosed. The fluid sample is applied to a lateral flow strip, and impedance of the strip is measured as the assay dries. Analysis of the drying-dependent impedance measurements indicates the presence and quantity of the analyte in the fluid sample.

Abstract: Systems, methods, devices and test kits for detecting an analyte and quantifying an analyte level in a biological fluid sample using a lateral flow assay with enhancement solution are disclosed. The fluid sample is applied to a lateral flow strip, and thereafter an enhancement solution is applied that enhances the results of the test. The enhancement solution is contained with the device, such as in a store or blister. The assay may also include a washing fluid applied to the strip in a similar manner.

Abstract: A chimeric protein comprises a redox catalytic domain from one source and an electron transfer domain from a different source. The protein is used in a method in which a substrate for the redox catalytic domain is acted on, electrons are transferred between the redox catalytic domain and the electron transfer domain and between the electron transfer domain and an electrode. The flow of current or potential at the electrode may be monitored to determine the presence or amount of a substrate which is an analyte of interest. Alternatively current may be driven through the electrode to drive reaction of the substrate, for instance to detoxify samples. The redox catalytic domain is suitably derived from a cytochrome P450, and the electron transfer domain may be flavodoxin.

Abstract: A chimeric protein comprises a redox catalytic domain from one source and an electron transfer A domain from a different source. The protein is used in a method in which a substrate for the redox catalytic domain is acted on, electrons are transferred between the redox catalytic domain and the electron transfer domain and between the electron transfer domain and an electrode. The flow of current or potential at the electrode may be monitored to determine the presence or amount of a substrate which is an analyte of interest. Alternatively current max be driven through the electrode to drive reaction of the substrate, for instance to detoxify samples. The redox catalytic domain is suitably derived from a cytochrome P450, and the electron transfer domain may be flavodoxin.

Abstract: A chimeric protein comprises a redox catalytic domain from one source and an electron transfer domain from a different source. The protein is used in a method in which a substrate for the redox catalytic domain is acted on, electrons are transferred between the redox catalytic domain and the electron transfer domain and between the electron transfer domain and an electrode. The flow of current or potential at the electrode may be monitored to determine the presence or amount of a substrate which is an analyte of interest. Alternatively current max be driven through the electrode to drive reaction of the substrate, for instance to detoxify samples. The redox catalytic domain is suitably derived from a cytochrome P450, and the electron transfer domain may be flavodoxin.

Abstract: A chimeric protein comprises a redox catalytic domain from one source and an electron transfer domain from a different source. The protein is used in a method in which a substrate for the redox catalytic domain is acted on, electrons are transferred between the redox catalytic domain and the electron transfer domain and between the electron transfer domain and an electrode. The flow of current or potential at the electrode may be monitored to determine the presence or amount of a substrate which is an analyte of interest. Alternatively current max be driven through the electrode to drive reaction of the substrate, for instance to detoxify samples. The redox catalytic domain is suitably derived from a cytochrome P450, and the electron transfer domain may be flavodoxin.

Abstract: A fluorescently labeled nucleic acid having a hairpin structure between the fluorophore label and a point of attachment to a solid phase is useful as a probe to detect nucleic acid from a sample. The solid phase quenches the fluorophore label when the hairpin structure exists but this quenching is relieved by duplex formation between probe and a sample oligonucleotide. Probes for specific nucleic acid sequences can be immobilized as arrays on solid phase surfaces for detection of multiple nucleic acid sequences simultaneously from electrophoresis gels and from aqueous solutions. These probes and methods for their use can be combined with known solid phases, particularly those used for plasmon surface detection and electron transfer detection of nucleic acid. The probes can be washed and reused, and have other advantageous features over known probe methods.