The invention is directed to a competitive glucose binding affinity assay comprising a glucose receptor (typically mannan binding lectin) labeled with an assay fluorophore and a modified glucose analog (typically dextran) labeled with a reference fluorophore. In certain embodiments, the glucose analog is dextran and is coupled to both a reference fluorophore and a quencher dye (e.g. hexamethoxy crystalviolet-1). Optionally the reference fluorophore is blue shifted relative to the assay fluorophore.

Disclosed herein are methods and systems for determining whether a cell is resistant to one or more drugs. Also, disclosed herein are methods and systems for monitoring the treatment of a cancer patient to determine whether the cancerous cells being treated are resistant to the treatment. Further, disclosed herein are methods and systems for predicting the responsiveness of a cell to a drug. Also, disclosed herein are methods and systems to determine the rate of the efficacy of a chemotherapeutic drug on a cancerous, neoplastic or damaged cells.

The present disclosure relates to glycan-based biomarkers for the diagnosis or prognosis of brain damage, such as traumatic brain injury (TBI).

Described herein are engineered microbe-targeting or microbe-binding molecules, kits comprising the same and uses thereof. Some particular embodiments of the microbe-targeting or microbe-binding molecules comprise a carbohydrate recognition domain of mannose-binding lectin, or a fragment thereof, linked to a portion of a Fc region. In some embodiments, the microbe-targeting molecules or microbe-binding molecules can be conjugated to a substrate, e.g., a magnetic microbead, forming a microbe-targeting substrate (e.g., a microbe-targeting magnetic microbead). Such microbe-targeting molecules and/or substrates and the kits comprising the same can bind and/or capture of a microbe and/or microbial matter thereof, and can thus be used in various applications, e.g., diagnosis and/or treatment of an infection caused by microbes such as sepsis in a subject or any environmental surface. Microbe-targeting molecules and/or substrates can be regenerated after use by washing with a low pH buffer or buffer in which calcium is insoluble.

The present invention provides a sandwich assay for quantifying a glycoprotein, which is a substance to be detected, in a sample using a labeled lectin, wherein the effect attributed to a contaminant, namely noise on the quantified value of the substance to be detected, is suppressed by introduction of a simple treatment. The sandwich assay includes a treatment for inhibiting the binding of the labeled lectin to a sugar chain carried by the contaminant non-specifically adsorbed to the measurement region, which contaminant is contained in the sample and which sugar chain is the same as that of the substance to be detected.

The invention is directed to a competitive glucose binding affinity assay comprising a glucose receptor (typically mannan binding lectin) labeled with an assay fluorophore and a modified glucose analog (typically dextran) labeled with a reference fluorophore. In certain embodiments, the glucose analog is dextran and is coupled to both a reference fluorophore and a quencher dye (e.g. hexamethoxy crystalviolet-1). Optionally the reference fluorophore is blue shifted relative to the assay fluorophore.

Disclosed herein are methods and kits for isolating and/or quantifying exosomes in a sample. For example, the exosomes are isolating using lectin-modified magnetic beads suspended in an exosome-free buffer, and the exosome-bead complexes are isolated from the remainder of the mixture using a magnetic field. For separating the exosomes from the exosome-bead complexes, an elution buffer having a pH value of 6.8 to 7.6 is used, thereby avoiding the convention elution steps involving acidic or alkaline reagents. For quantification, the exosome-bead complexes, as isolated, are subject to subsequent flow cytometry.

A purpose of the present invention is to provide a highly sensitive and less expensive lectin-immobilized base material (for example, a lectin plate), said lectin-immobilized base material having stable qualities and being able to be sufficiently washed after a target sugar chain-containing antigen binds thereto. Another purpose of the present invention is to provide a method for immobilizing lectin to a base material therefor. Provided are: a method whereby a lectin-peptide fusion, in which a peptide capable of adsorbing to a base material surface such as a PS tag is fused with the N-terminal side or C-terminal side of lectin capable of recognizing a target sugar chain, is immobilized on the peptide side to a base material; and a lectin-immobilized base material produced by this method. By using the lectin-immobilized base material, a target sugar chain-containing antigen can be highly sensitively and evenly measured and, moreover, target sugar chain-containing cells, etc. can be separated (concentrated and harvested).

To provide a device capable of cancer diagnosis with high sensitivity and specificity, a cancer diagnosis device (1) includes: an extracellular vesicle capturing section (16 to 18) including immobilization supports on which lectins are immobilized respectively, the lectins being each capable of binding specifically to a surface sugar chain included in an extracellular vesicle derived from a cancer cell, the immobilization supports corresponding respectively to one or more kinds of the surface sugar chain; and a detecting section configured to detect a microRNA included in the extracellular vesicle.

[Problem] To provide a method that increases the detection level of a reaction product generated through a reaction between a glycoprotein and a carbohydrate-binding compound in order to detect the glycoprotein with high precision.

[Solution] A method for detecting a glycoprotein according to the present invention comprising the steps of: subjecting a sample containing the glycoprotein to a protease treatment; allowing the protease-treated glycoprotein to react with a sugar-binding compound having affinity with a glycan contained in the glycoprotein in order to obtain a reaction product between the glycoprotein and the sugar-binding compound; and detecting the reaction product. The sugar-binding compound is preferably a sugar-binding protein.