Provided herein are systems, devices and methods for the rapid and accurate measurement of analyte particles binding-induced aggregation of reporter particles. In the presence of analyte particles of interest, reporter particles form aggregates which increase in mean particle size as the concentration of analyte increases. From analysis of the mean particle size, determined from sample frames, the presence and/or concentration of analyte can be determined.

A linker molecule and method for treating a substrate surface is provided, which includes a linker molecule with a plurality of moieties capable of resisting non-specific binding of proteins whilst permitting specific binding of a target biomolecule or a biomolecule of interest, including antibodies.

A linker molecule and method for treating a substrate surface is provided, which includes a linker molecule with a plurality of moieties capable of resisting non-specific binding of proteins whilst permitting specific binding of a target biomolecule or a biomolecule of interest, including antibodies.

Provided is a highly sensitive and less expensive lectin-immobilized base material (for example, a lectin plate), such as lectin-immobilized base material having stable qualities and being able to be sufficiently washed after a target sugar chain-containing antigen binds thereto. Further provided is a method for immobilizing lectin to a base material therefor. Particularly provided are: a method whereby a lectin-peptide fusion, in which a peptide capable of adsorbing to a base material surface such as a polystyrene (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).

Provided is a highly sensitive and less expensive lectin-immobilized base material (for example, a lectin plate), such as lectin-immobilized base material having stable qualities and being able to be sufficiently washed after a target sugar chain-containing antigen binds thereto. Further provided is a method for immobilizing lectin to a base material therefor. Particularly provided are: a method whereby a lectin-peptide fusion, in which a peptide capable of adsorbing to a base material surface such as a polystyrene (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).

Provided are methods of preparing a sample for detection by placing the sample on a shrinkable scaffold and then shrinking the scaffold. An exemplary shrinkable scaffold is a thermoplastic substrate.

Provided are methods of preparing a sample for detection by placing the sample on a shrinkable scaffold and then shrinking the scaffold. An exemplary shrinkable scaffold is a thermoplastic substrate.

Disclosed is a method for live detection of apoptotic sperms contained in a sperm sample under in vitro conditions.

Disclosed is a method for live detection of apoptotic sperms contained in a sperm sample under in vitro conditions.

Provided herein are materials and methods for performing bioluminescent assays using a bifunctional probe. In particular, the present disclosure provides compositions and methods for detecting and/or quantifying a biomolecule and/or assaying a cellular process associated with the biomolecule using a bifunctional probe capable of binding the biomolecule and generating a bioluminescent and/or fluorescent signal.