The present invention relates to a two-photon fluorescent probe compound represented by Chemical Formula 1 below, and a method for imaging amyloid beta plaques using same, wherein the two-photon fluorescent probe compound according to the present invention maintains an excellent two-photon fluorescence cross-section while at the same time maintaining efficient BBB permeability by minimizing background fluorescence such that a high signal-to-noise ratio is exhibited, and can effectively image Aβ plaques since high selectivity and sensitivity to Aβ plaques are exhibited, and can thus be usefully used in the field of neurodegenerative disease research, including early diagnosis and treatment of Alzheimer's disease. [Chemical Formula 1]

The present invention addresses a problem of providing a method for collecting extracellular vesicles derived from nervous system cells at an improved efficiency.

This problem is solved by a method for collecting extracellular vesicles derived from nervous system cells, said method comprising a step for mixing an anti-APLP1 antibody with a sample containing extracellular vesicles to form anti-APLP1 antibody-extracellular vesicle complexes and a step for collecting the anti-APLP1 antibody-extracellular vesicle complexes.

The present invention is directed to polymerized products and compositions useful for the treatment and prevention of amyloid disease in a subject. The invention further relates to isolated antibodies that recognize a common conformational epitope of amyloidogenic proteins or peptides that are useful for the diagnosis, treatment, and prevention of amyloid disease.

Described herein are devices and methods for simultaneously expressing amyloid precursor protein and TonB protein. These devices and methods increase the production of these two proteins while also minimizing costs, making the proteins more widely accessible for medical research purposes, including the development of diagnostic tests for numerous diseases associated with elevated production of amyloid proteins. The amyloid precursor protein and TonB produced by the devices and methods described herein, as well as the devices themselves, can be used in experiments designed to model the interactions between metals and amyloids such as β-amyloid that are characteristic of numerous diseases such as Alzheimer's. Finally, provided herein are diagnostic tests that can detect Alzheimer's disease in samples from patients; the tests are sensitive enough to identify diseases such as Alzheimer's even at pre-clinical stages, before the appearance of symptoms.

A method for the pre-amplification sample processing of a prion or other amyloid converting protein in a sample. A key feature of the assay is its ability to amplify and thus detect small quantities of the abnormally folded ‘seed’ forms of misfolded proteins. The assay also opens up the ability to quantify the amount of “seed” present. The methods facilitate the early detection of diseases associated with misfolded proteins, as well as assessment of therapies against these diseases. The method can detect amyloid seeding activity (prions) in blood samples, including the buffy coat cells harvested from pre-clinical and clinical subjects. These findings further enhance the ability to assess the longitudinal course of prion disease and the role hematogenous prions play in pathogenesis. We demonstrate the ability to detect prions in as few as 5×10.sup.5 buffy coat cells by lipase-iron oxide bead-RT-QuIC performed at 42° C. (LIQ42) in 79% of CWD-biopsy positive WTD, which increased to 100% when LIQ was performed at 55° C. (LIQ55). RT-QuIC assessment of PMCA (PQ) round 5 product revealed hematogenous prions in 92% of the WTD.

The present invention provides a method for screening a substance that controls APP669 N-terminal cleavage activity, the method comprising: causing a candidate substance to act on a cultured cell; measuring an AP-related peptide produced from the cultured cell; and evaluating APP669 N-terminal cleavage activity. The candidate substance is selected, for example, from the group consisting of a low molecular weight compound, a peptide, a protein, and a nucleic acid. The present invention also provides an APP669 N-terminal cleavage enzyme containing ADAMTS4.

Disclosed are an immunoassay method capable of highly sensitively measuring amyloid β in a blood sample, and a kit therefor. The immunoassay method for amyloid β is a method of immunoassay of amyloid β in a blood sample, wherein the immunoassay is carried out in the presence of an anionic polymer such as a dextran sulfate salt or a polystyrene sulfonic acid salt. The kit for immunoassay of amyloid β in a blood sample comprises: an anti-amyloid β antibody or an antigen-binding fragment thereof; and an anionic polymer.

The disclosure pertains to antibodies that bind A-beta oligomers and methods of using said antibodies. Also provided are chimeric or humanized antibodies, including antibodies having specific CDRs identified herein, or a sequence with at least 80% sequence identity to specific VH sequences identified herein, optionally wherein the CDR H3 amino acid sequence is as set forth in any one of SEQ ID NOs: 31-36, 38-40, or 42-50. Also provided are methods and uses thereof as well as kits comprising said antibodies.

The present disclosure relates to methods of measuring and analyzing phosphorylation sites in the tau protein and determining correlations with other biomarkers of Alzheimer's disease and tauopathies.

Disclosed is a specimen analysis method for analyzing a specimen regarding a plurality of measurement items, the specimen analysis method comprising: measuring a first measurement item and a second measurement item on the basis of a measurement order; executing a process related to a time difference between a measurement of the first measurement item and a measurement of the second measurement item; and obtaining a calculation value from a measurement value of the first measurement item and a measurement value of the second measurement item.