Abstract: The present invention relates to a method for detection of binding or interaction events between a binding agent and its corresponding analyte (such as an antibody and an antigen) in which a signal is detected which is substantially more amplified and thus easier to detect than in prior art systems. The method comprises simultaneous but separate addition of a first enhancement reagent having affinity for said analyte and a second enhancement reagent having affinity for the first enhancement reagent wherein the first enhancement reagent binds to the analyte and the second enhancement reagent binds to the first enhancement reagent, and, wherein the first and second enhancement reagents have more than one binding site so that they are able to bind to each other to thereby amplify a detectable signal from the binding event.

Abstract: The present invention relates to a method for detection of binding or interaction events between a binding agent and its corresponding analyte (such as an antibody and an antigen) in which a signal is detected which is substantially more amplified and thus easier to detect than in prior art systems. The method comprises simultaneous but separate addition of a first enhancement reagent having affinity for said analyte and a second enhancement reagent having affinity for the first enhancement reagent wherein the first enhancement reagent binds to the analyte and the second enhancement reagent binds to the first enhancement reagent, and, wherein the first and second enhancement reagents have more than one binding site so that they are able to bind to each other to thereby amplify a detectable signal from the binding event.

Abstract: A method of determining the total concentration of an analyte in a fluid sample, wherein at least part of the analyte is present as a complex with an analyte-binding species. The methods includes the steps of: a) subjecting the sample to conditions that reduce the binding affinity between analyte and analyte-binding species sufficiently to dissociate substantially any analyte complex and provide substantially all analyte in free form, b) subjecting the sample to conditions that restore the binding affinity between analyte and analyte-binding species, and c) immediately after the binding affinity has been restored, and before any substantial re-complexing of the analyte has taken place, determining the concentration of free analyte in the sample. A method of determining the concentration of complex-bound analyte in a sample is also disclosed.

Abstract: A method of preparing a protein-resistant reactive solid support surface is disclosed. The method comprises the steps of providing a solid support having a hydrogel coating with a plurality of binding elements, coupling a protein resistant compound to the hydrogel via a first fraction of the binding elements, and coupling at least one binding agent to the hydrogel via a second fraction of the binding elements, whereby the protein resistant compound and the at least one binding agent are co-immobilized to the hydrogel. Also the use of the reactive surface in analysis, such as immunogenicity assays, is disclosed.

Abstract: A method of determining the concentration of a virus or antigen thereof in a sample comprises the steps of: providing a sensor surface having immobilized thereto a virus antigen or a virus antigen analogue, mixing the sample with a known amount of antibody to the virus antigen to obtain a predetermined concentration of antibody to the antigen in the sample mixture, contacting the sample mixture with the sensor surface to bind free antibody in the mixture to the sensor surface, measuring the response of the sensor surface to the binding of free antibody, and determining the concentration of the virus or antigen in the sample from a calibration curve prepared by measuring the responses obtained for mixtures containing the predetermined concentration of antibody and different concentrations of virus.

Abstract: A method of determining the total concentration of an analyte in a fluid sample, wherein at least part of the analyte is present as a complex with an analyte-binding species. The methods includes the steps of: a) subjecting the sample to conditions that reduce the binding affinity between analyte and analyte-binding species sufficiently to dissociate substantially any analyte complex and provide substantially all analyte in free form, b) subjecting the sample to conditions that restore the binding affinity between analyte and analyte-binding species, and c) immediately after the binding affinity has been restored, and before any substantial re-complexing of the analyte has taken place, determining the concentration of free analyte in the sample. A method of determining the concentration of complex-bound analyte in a sample is also disclosed.

Abstract: A method of preparing a protein-resistant reactive solid support surface is disclosed. The method comprises the steps of providing a solid support having a hydrogel coating with a plurality of binding elements, coupling a protein resistant compound to the hydrogel via a first fraction of the binding elements, and coupling at least one binding agent to the hydrogel via a second fraction of the binding elements, whereby the protein resistant compound and the at least one binding agent are co-immobilized to the hydrogel. Also the use of the reactive surface in analysis, such as immunogenicity assays, is disclosed.

Abstract: A method of preparing a protein-resistant reactive solid support surface is disclosed. The method comprises the steps of providing a solid support having a hydrogel coating with a plurality of binding elements, coupling a protein resistant compound to the hydrogel via a first fraction of the binding elements, and coupling at least one binding agent to the hydrogel via a second fraction of the binding elements, whereby the protein resistant compound and the at least one binding agent are co-immobilized to the hydrogel. Also the use of the reactive surface in analysis, such as immunogenicity assays, is disclosed.

Abstract: A method of determining the binding of an oligonucleotide probe to a test nucleic acid sequence comprises the steps of: (a) providing the test nucleic acid sequence in single-stranded form, (b) contacting the test nucleic acid sequence under hybridizing conditions with a solution containing an oligonucleotide probe which is complementary to a defined portion of a standard nucleic acid sequence, (c) immobilizing to a solid support a nucleic acid fragment at least part of which is complementary to said oligonucleotide probe, (d) contacting the solution from step (b) with said solid support, and (e) determining the amount of binding of oligonucleotide probe present in said solution to its complementary nucleic acid fragment on the second solid support, said amount being inversely related to the amount of binding of the oligonucleotide probe to the test nucleic acid sequence.

Abstract: In assays of the type which comprise contacting the sample containing the analyte to be detected with a solid phase surface supporting a ligand capable of binding the analyte, undesired binding to the surface is prevented to a substantial degree by adding to the sample one or more components of the material forming the ligand supporting solid phase surface, which components are in at least partially soluble form and capable of interacting with constituents of the sample medium.

Abstract: A method of characterizing a macromolecule by studying its interactions with ligands comprises the determination of the mutual influence of ligand interactions by, after the macromolecule has interacted with at least one ligand, contacting the macromolecule with at least one additional ligand, either the macromolecule or the additional ligand or ligands having been bound to a sensor surface, determining interaction by detecting a consequential change in the physico-chemical properties of the sensor surface, and on the basis of the determined mutual dependence between the ligand interactions discriminating between epitopes of the macromolecule and mapping their relative positions.