Abstract: The present disclosure relates to a method for detecting a core polypeptide of a hepatitis C virus (HCV) in a sample from a subject with the steps of (a) contacting the sample with a surfactant comprising a cationic detergent; (b) contacting the sample with a binding compound; and (c) detecting a core polypeptide of the HCV in the sample; wherein step a) is immediately followed by step b). The present disclosure further relates to a method for pre-processing a sample from a subject for detection of an HCV core polypeptide, involving (a) contacting the sample with a surfactant comprising a cationic detergent and, optionally, with an agent inducing a pH shift, immediately followed by (b) contacting the sample with a binding compound. Moreover, the present disclosure further relates to uses, devices, and analytical systems related to aforesaid methods.

Abstract: The present disclosure relates to a method for detecting a core polypeptide of a hepatitis C virus (HCV) in a sample from a subject involving (a) contacting said sample with a base and with a surfactant having a cationic detergent, and (b) detecting a core polypeptide of the HCV in the sample. The present invention further relates to a method for pre-processing a sample from a subject for detection of HCV, involving contacting the sample with a base and with a surfactant having a cationic detergent; and to a pre-processing reagent for detecting HCV in a sample, having a base and a surfactant including a cationic detergent, wherein the surfactant also has a nonionic detergent. Moreover, the present disclosure further relates to kits, uses, and devices related to the methods disclosed.

Abstract: The disclosure concerns a method and kits for measurement of an analyte in a microparticle-based analyte-specific binding assay. In the assay, the microparticles are coated with the first partner of a binding pair, mixing the coated microparticles and at least two analyte-specific binding agents, each conjugated to the second partner of the binding pair, and a sample suspected of containing the analyte. The second partner of the binding pair is bound to each of the analyte-specific binding agents via a linker comprising from 12 to 30 ethylene glycol units (PEG 12 to 30), thereby binding the analyte via the conjugated analyte-specific binding agents to the coated microparticles. The method also entails separating the microparticles having the analyte bound via the binding pair and the analyte-specific binding agent from the mixture and measuring the analyte bound to the microparticles.

Abstract: The disclosure relates to a multi-epitope fusion protein as well as to its use as calibrator and/or control in an in vitro diagnostics immunoassay for detecting HCV core antigen. The multi-epitope fusion protein has two to six different non-overlapping linear peptides present in the amino acid sequence of hepatitis C virus (HCV) core protein, wherein each of the peptides is separated from the other peptides by a spacer consisting of a non-HCV amino acid sequence and having a chaperone amino acid sequence. No further HCV specific amino acid sequences are present in the polypeptide. A further aspect relates to a reagent kit for detecting HCV core antigen containing said multi-epitope fusion protein as calibrator or control or both.

Abstract: The disclosure relates to a multi-epitope fusion protein as well as to its use as calibrator and/or control in an in vitro diagnostics immunoassay for detecting HCV core antigen. The multi-epitope fusion protein has two to six different non-overlapping linear peptides present in the amino acid sequence of hepatitis C virus (HCV) core protein, wherein each of the peptides is separated from the other peptides by a spacer consisting of a non-HCV amino acid sequence and having a chaperone amino acid sequence. No further HCV specific amino acid sequences are present in the polypeptide. A further aspect relates to a reagent kit for detecting HCV core antigen containing said multi-epitope fusion protein as calibrator or control or both.

Abstract: The disclosure concerns a method and kits for measurement of an analyte in a microparticle-based analyte-specific binding assay. In the assay, the microparticles are coated with the first partner of a binding pair, mixing the coated microparticles and at least two analyte-specific binding agents, each conjugated to the second partner of the binding pair, and a sample suspected of containing the analyte. The second partner of the binding pair is bound to each of the analyte-specific binding agents via a linker comprising from 12 to 30 ethylene glycol units (PEG 12 to 30), thereby binding the analyte via the conjugated analyte-specific binding agents to the coated microparticles. The method also entails separating the microparticles having the analyte bound via the binding pair and the analyte-specific binding agent from the mixture and measuring the analyte bound to the microparticles.

Abstract: The present disclosure relates to a method for detecting a core polypeptide of a hepatitis C virus (HCV) in a sample from a subject with the steps of (a) contacting the sample with a surfactant comprising a cationic detergent; (b) contacting the sample with a binding compound; and (c) detecting a core polypeptide of the HCV in the sample; wherein step a) is immediately followed by step b). The present disclosure further relates to a method for pre-processing a sample from a subject for detection of an HCV core polypeptide, involving (a) contacting the sample with a surfactant comprising a cationic detergent and, optionally, with an agent inducing a pH shift, immediately followed by (b) contacting the sample with a binding compound. Moreover, the present disclosure further relates to uses, devices, and analytical systems related to aforesaid methods.

Abstract: The present disclosure relates to a method for detecting a core polypeptide of a hepatitis C virus (HCV) in a sample from a subject involving (a) contacting said sample with a base and with a surfactant having a cationic detergent, and (b) detecting a core polypeptide of the HCV in the sample. The present invention further relates to a method for pre-processing a sample from a subject for detection of HCV, involving contacting the sample with a base and with a surfactant having a cationic detergent; and to a pre-processing reagent for detecting HCV in a sample, having a base and a surfactant including a cationic detergent, wherein the surfactant also has a nonionic detergent. Moreover, the present disclosure further relates to kits, uses, and devices related to the methods disclosed.

Abstract: Methods for determining an analyte in a sample by immunoassay in a one-step format without performing washing steps are described. The method includes a first analyte-specific receptor that contains at least two binding sites for the analyte, and a second analyte-specific receptor that selectively binds to an aggregate arrangement of at least two analyte molecules bound to the first receptor.

Abstract: The invention relates to soluble rubella E1 antigens and variants of these antigens. The antigens contain amino acids 201 to 432 or 169 to 432 and are lacking amino acids 453 to 481 as well as at least the amino acids 143 to 164. They further contain a region spanning two disulfide-bridges. The invention also relates to a recombinant DNA molecule encoding the rubella E1 antigens, the expression of rubella E1 antigens as chaperone fusion proteins and their use in a method of detecting antibodies against rubella in a sample.

Abstract: The invention relates to a method for determining an analyte in a sample by means of an assay that can be carried out in a one-step format without performing washing steps. The method includes a first analyte-specific receptor that contains at least one bonding point for the analyte, e.g., several antibodies on a particle, as well as a second analyte-specific receptor that can selectively bond to an arrangement comprising at least two analyte molecules which are bound to the first receptor. An antibody sandwich immune assay is described in which the detection is based on electrochemiluminescence.

Abstract: The invention relates to soluble rubella E1 antigens and variants of these antigens. The antigens contain amino acids 201 to 432 or 169 to 432 and are lacking amino acids 453 to 481 as well as at least the amino acids 143 to 164. They further contain a region spanning two disulfide-bridges. The invention also relates to a recombinant DNA molecule encoding the rubella E1 antigens, the expression of rubella E1 antigens as chaperone fusion proteins and their use in a method of detecting antibodies against rubella in a sample.

Abstract: A soluble rubella E1 antigen variant is disclosed that comprises amino acids 334-409 of the native rubella E1 peptide, but lacks the C-terminal end and at least the transmembrane region and the anchor segment as well as at least the amino acids 143 to 164. Also described is a recombinant DNA molecule encoding the rubella E1 antigen variants which are recombinantly expressed as a chaperone fusion protein, refolded into a soluble and immunoreactive conformation, and further used for the serological detection of anti-rubella antibodies. In addition, also disclosed is a method for the detection, determination and quantification of anti-rubella antibodies of IgG and/or IgM subclass in a sample wherein the rubella E1 antigen is used as a capture reagent and/or binding partner for the antibodies.

Abstract: The invention disclosed relates to a soluble rubella E1 antigen and variants of this peptide characterized by lacking at the C-terminal end at least the transmembrane region and the anchor segment as well as at least the amino acids 143 to 164 and containing at least the region spanning the disulfide bridges Cys 349-Cys 352 and Cys 368-401 whereas the N-terminus (Cys 349) of this region contains additionally at least 15 amino acids and/or the C-terminus (Cys 401) of this region contains additionally at least 8 amino acids of the adjacent rubella E1 antigen sequence. Also described are a recombinant DNA molecule encoding the rubella E1 antigen and variants which are recombinantly expressed as a chaperone fusion protein, refolded into a soluble and immunoreactive conformation, and further used for the serological detection of anti-rubella antibodies.