G01N33/547

SPR-based dual-binding assay for the functional analysis of multispecific molecules

Herein is reported a method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the steps of capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the first or the second antigen to form a captured antibody-antigen complex and determining a first binding signal, either i) incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal, or ii) regenerating the surface, capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the antigen not used for the formation of the captured antibody-antigen complex in step b) to form a captured antibody-antigen-antigen complex and determining a third binding signal, and determining the overall or individual binding of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal.

SPR-based dual-binding assay for the functional analysis of multispecific molecules

Herein is reported a method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the steps of capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the first or the second antigen to form a captured antibody-antigen complex and determining a first binding signal, either i) incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal, or ii) regenerating the surface, capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the antigen not used for the formation of the captured antibody-antigen complex in step b) to form a captured antibody-antigen-antigen complex and determining a third binding signal, and determining the overall or individual binding of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal.

DEVICES AND METHODS FOR PLASMA SEPARATION AND METERING

Devices, assemblies, and kits are disclosed for separating and/or metering a plasma sample from a patient's liquid test sample. Also disclosed are methods of producing and using same.

DEVICES AND METHODS FOR PLASMA SEPARATION AND METERING

Devices, assemblies, and kits are disclosed for separating and/or metering a plasma sample from a patient's liquid test sample. Also disclosed are methods of producing and using same.

CROSS-LINKED PRODUCT OF AMYLOID-B PROTEIN (AB) AS POTENTIAL SUBSTITUTE FOR AMYLOSPHEROIDS (ASPD) AND ANALYSIS OF ASPD

A substance that can be a substitute for amylospheroids (ASPD) and a method for analyzing ASPD are provided. Viewed from one aspect, the present disclosure relates to a substance in which amyloid-β protein (Aβ) is cross-linked with a cross-linking agent that has a spacer arm length of between 4 Å and 50 Å inclusive or a cross-linking agent that has, as a spacer arm, not less than 1 and not more than 13 groups that are an oxyethylene group(s) (—CH.sub.2CH.sub.2O—) and/or an oxypropylene group(s) (—CH.sub.2CH.sub.2CH.sub.3O—). Viewed from another aspect, the present disclosure relates to a method for analyzing ASPD using the substance as a reference material.

CROSS-LINKED PRODUCT OF AMYLOID-B PROTEIN (AB) AS POTENTIAL SUBSTITUTE FOR AMYLOSPHEROIDS (ASPD) AND ANALYSIS OF ASPD

A substance that can be a substitute for amylospheroids (ASPD) and a method for analyzing ASPD are provided. Viewed from one aspect, the present disclosure relates to a substance in which amyloid-β protein (Aβ) is cross-linked with a cross-linking agent that has a spacer arm length of between 4 Å and 50 Å inclusive or a cross-linking agent that has, as a spacer arm, not less than 1 and not more than 13 groups that are an oxyethylene group(s) (—CH.sub.2CH.sub.2O—) and/or an oxypropylene group(s) (—CH.sub.2CH.sub.2CH.sub.3O—). Viewed from another aspect, the present disclosure relates to a method for analyzing ASPD using the substance as a reference material.

Carbon Nanohorns/Nafion/Fe3O4@Pd immunosensor for Shrimp Tropomyosin

The present application discloses an electrochemiluminescence immunosensor. The immunosensor includes an electrode functionalized by a nanocomposite film. The film further includes carbon nanohorns dispersed in Nafion® perfluorinated resin solution. The polymeric solution is further stabilized by magnetic nanoparticles. The immunosensor is a Point of care (POC)-based. The immunosensor is configured to work in the range from 100 ng/mL to 1 fg/mL, and has tendency to detect even traces of the tropomyosin. The immunosensor is capable to detect traces even less than 1 fg/mL, hence having high specificity for Tro-Ag detection in food products with distinguished repeatability.

Carbon Nanohorns/Nafion/Fe3O4@Pd immunosensor for Shrimp Tropomyosin

The present application discloses an electrochemiluminescence immunosensor. The immunosensor includes an electrode functionalized by a nanocomposite film. The film further includes carbon nanohorns dispersed in Nafion® perfluorinated resin solution. The polymeric solution is further stabilized by magnetic nanoparticles. The immunosensor is a Point of care (POC)-based. The immunosensor is configured to work in the range from 100 ng/mL to 1 fg/mL, and has tendency to detect even traces of the tropomyosin. The immunosensor is capable to detect traces even less than 1 fg/mL, hence having high specificity for Tro-Ag detection in food products with distinguished repeatability.

SILICA SHELL ENCAPSULATED POLYAROMATIC-CORE MICROPARTICLES
20220404344 · 2022-12-22 ·

The present invention provides silica shell encapsulated polyaromatic-core microparticles and methods for producing and using the same. In particular, the silica shell encapsulated polyaromatic-core microparticles of the invention are hydrophilic microparticle scintillators comprising (i) polyaromatic-core microparticle (1), wherein said polyaromatic-core microparticle (1) is doped with a scintillator material (2); and (ii) a silica-shell portion (3) encapsulating said polyaromatic-core microparticle (1), wherein said silica-shell portion (3) comprises an outer surface (4). The polyaromatic-core portion is formed from an aromatic vinyl compound selected from the group consisting of styrene, vinyl toluene, and a mixture thereof.

SILICA SHELL ENCAPSULATED POLYAROMATIC-CORE MICROPARTICLES
20220404344 · 2022-12-22 ·

The present invention provides silica shell encapsulated polyaromatic-core microparticles and methods for producing and using the same. In particular, the silica shell encapsulated polyaromatic-core microparticles of the invention are hydrophilic microparticle scintillators comprising (i) polyaromatic-core microparticle (1), wherein said polyaromatic-core microparticle (1) is doped with a scintillator material (2); and (ii) a silica-shell portion (3) encapsulating said polyaromatic-core microparticle (1), wherein said silica-shell portion (3) comprises an outer surface (4). The polyaromatic-core portion is formed from an aromatic vinyl compound selected from the group consisting of styrene, vinyl toluene, and a mixture thereof.