The present disclosure is directed to antibody-linked immuno-sedimentation agent, the antibody being linked to a sedimentation agent by a non-antigen binding region of the antibody, and a method of isolating a target from a sample using the antibody-linked immuno-sedimentation agent. The methods involve forming a mixture including a sample with an antibody linked immuno-sedimentation agent and red blood cells under conditions sufficient to form red blood cell rouleaux and allow antibody-antigen binding.

Assays and methods for verifying the validity of a urine sample submitted for Drugs of Abuse (DOA) testing. Embodiments include a SUD Diagnostic Panel that includes six assays: specific gravity index assay, long-duration counterfeit urine assay, short-duration counterfeit urine assay, oxidant history assay, pH assay, and creatinine assay. The SUD Diagnostic Panel detects twelve principle classes of adulteration. Detection of adulteration of one or more urine samples from a patient indicates an attempt to subvert test results and provides an objective indication in one instance and an object diagnosis in another instance of SUD.

Assays and methods for verifying the validity of a urine sample submitted for Drugs of Abuse (DOA) testing. Embodiments include a SUD Diagnostic Panel that includes six assays: specific gravity index assay, long-duration counterfeit urine assay, short-duration counterfeit urine assay, oxidant history assay, pH assay, and creatinine assay. The SUD Diagnostic Panel detects twelve principle classes of adulteration. Detection of adulteration of one or more urine samples from a patient indicates an attempt to subvert test results and provides an objective indication in one instance and an object diagnosis in another instance of SUD.

A method of solvent-induced protein precipitation (SIP) for detecting the interaction of ligands with proteins in a complex protein sample. After the equal amount of solvent is added to the protein samples with and without a ligand to denature and precipitate the proteins, the protein abundances in supernatant and/or precipitate in the ligand group and the control group are measured by quantitative technology. The target protein(s) of a ligand is/are determined by comparing the differences of protein abundances in the ligand group and the control group. The affinity between a ligand and its targets can be evaluated by dose dependent experiments. This method does not require the chemical modification of the ligand and has the feature of high specificity. Furthermore, in certain embodiments, the targets identified by SIP method are complementary to those identified by thermal proteome profiling (TPP) method.

The present invention relates to methods that utilize a combination of immunoassay and magnetic immunoassay techniques to detect an analyte within an extended range of specified concentrations. In particular, a method includes forming, in a biological sample, a first complex of signal antibodies and analyte, and a second complex of the first complex and capture antibodies immobilized on magnetic beads, and contacting a first immunosensor with the biological sample to form a third complex localized on or near a surface of the first immunosensor. The first immunosensor includes an immobilized layer of capture antibodies configured to bind to the analyte, and the third complex includes the first complex bound to the immobilized layer of capture antibodies. The method further includes contacting a magnetic field localized around a second immunosensor with the biological sample such that the second complex is localized on or near a surface of the second immunosensor.

The present invention relates to methods that utilize a combination of immunoassay and magnetic immunoassay techniques to detect an analyte within an extended range of specified concentrations. In particular, a method includes forming, in a biological sample, a first complex of signal antibodies and analyte, and a second complex of the first complex and capture antibodies immobilized on magnetic beads, and contacting a first immunosensor with the biological sample to form a third complex localized on or near a surface of the first immunosensor. The first immunosensor includes an immobilized layer of capture antibodies configured to bind to the analyte, and the third complex includes the first complex bound to the immobilized layer of capture antibodies. The method further includes contacting a magnetic field localized around a second immunosensor with the biological sample such that the second complex is localized on or near a surface of the second immunosensor.

The systems and methods contained herein are directed toward automated analysis of agglutination reactions to determine properties of materials, including viruses and vaccines thereto. Advanced digital imaging and processing techniques are used to determine the presence or absence of viruses or antibodies within a fluid sample. The systems and methods are versatile, and can be used to determine specific properties of biomaterials and viruses, such as titer value, concentration, genotype, phenotype, serotype, vaccine efficacy, viral resistance and other properties of relevance in the medical, research and development fields. Also provided are systems and methods of standardization, repeatability, and data storage and transmittal to reduce errors and subjectivity inherent to conventional assays characterized by human readers.

The systems and methods contained herein are directed toward automated analysis of agglutination reactions to determine properties of materials, including viruses and vaccines thereto. Advanced digital imaging and processing techniques are used to determine the presence or absence of viruses or antibodies within a fluid sample. The systems and methods are versatile, and can be used to determine specific properties of biomaterials and viruses, such as titer value, concentration, genotype, phenotype, serotype, vaccine efficacy, viral resistance and other properties of relevance in the medical, research and development fields. Also provided are systems and methods of standardization, repeatability, and data storage and transmittal to reduce errors and subjectivity inherent to conventional assays characterized by human readers.

The present invention relates to methods that utilize a combination of immunoassay and magnetic immunoassay techniques to detect an analyte within an extended range of specified concentrations. In particular, a method includes forming, in a biological sample, a first complex of signal antibodies and analyte, and a second complex of the first complex and capture antibodies immobilized on magnetic beads, and contacting a first immunosensor with the biological sample to form a third complex localized on or near a surface of the first immunosensor. The first immunosensor includes an immobilized layer of capture antibodies configured to bind to the analyte, and the third complex includes the first complex bound to the immobilized layer of capture antibodies. The method further includes contacting a magnetic field localized around a second immunosensor with the biological sample such that the second complex is localized on or near a surface of the second immunosensor.

The present invention relates to methods that utilize a combination of immunoassay and magnetic immunoassay techniques to detect an analyte within an extended range of specified concentrations. In particular, a method includes forming, in a biological sample, a first complex of signal antibodies and analyte, and a second complex of the first complex and capture antibodies immobilized on magnetic beads, and contacting a first immunosensor with the biological sample to form a third complex localized on or near a surface of the first immunosensor. The first immunosensor includes an immobilized layer of capture antibodies configured to bind to the analyte, and the third complex includes the first complex bound to the immobilized layer of capture antibodies. The method further includes contacting a magnetic field localized around a second immunosensor with the biological sample such that the second complex is localized on or near a surface of the second immunosensor.