The present invention relates to a method for the evaluation of binding affinity of biologically active substances for cardiolipin based on acridinium salt utilization as a fluorescent probe.

The present invention relates to a labeled chimeric non-therapeutic antibodylike protein comprising, in a hypervariable region thereof, an enzyme cleavable peptide sequence derived from a hypervariable region of a reference therapeutic antibody.

Disclosed is a method for determining a blood specimen, comprising preparing a first measurement sample by mixing a blood specimen of a subject with a first coagulation time measurement reagent and measuring first coagulation time, preparing a second measurement sample by mixing the blood specimen with a second coagulation time measurement reagent and measuring second coagulation time, and acquiring a value based on the first coagulation time and the second coagulation time, wherein the second coagulation time measurement reagent contains a metal ion and/or normal plasma, and the value is used to determine whether the blood specimen of a subject is a blood specimen containing a lupus anticoagulant or a blood specimen containing a direct anticoagulant.

A memristive/memcapacitive device with vertex double-helical polarized biomimetic protein nanotubules forming double membranes with potential gradient mimicking mitochondria's inner double membrane was invented. The memristive/memcapacitive device comprises a cross-linked conductive organic polymer having a single-wall cross-bar polarized nanotube self-assembling membrane (SAM) on a gold chip with a minimum 5 nm space between the nanotubes. Under an applied potential, a pair of vertex double-helical circular current flow induced the Fermi arcs states promoting a direct chelating with zinc ions of the Matrix Metalloproteinase (MMP-2), that made a dual-functioning direct ultrasensitive detection of protein in an attomolar concentration possible without a procedure of cycteine switch under label-free, probe-free and reagent-free conditions. The energy harvesting feature is also disclosed.

The present invention relates to a labeled chimeric non-therapeutic antibodylike protein comprising, in a hypervariable region thereof, an enzyme cleavable peptide sequence derived from a hypervariable region of a reference therapeutic antibody

Extraction and separation methods that can be used to quantify the absolute concentrations of one or more low abundance biomolecules present in biological fluids and tissues, without the need for antibody enrichment or reliance on an antibody for quantification are provided. These biomolecules can be biomarkers used to diagnose and monitor disease progression. As an example, these methods are applied to human plasma and CSF, and used to quantify Alzheimer's disease biomarkers.

Disclosed is a method for determining a blood specimen, comprising preparing a first measurement sample by mixing a blood specimen of a subject with a first coagulation time measurement reagent and measuring first coagulation time, preparing a second measurement sample by mixing the blood specimen with a second coagulation time measurement reagent and measuring second coagulation time, and acquiring a value based on the first coagulation time and the second coagulation time, wherein the second coagulation time measurement reagent contains a metal ion and/or normal plasma, and the value is used to determine whether the blood specimen of a subject is a blood specimen containing a lupus anticoagulant or a blood specimen containing a direct anticoagulant.