G01N33/561

Wash for electrophoresis
12339248 · 2025-06-24 · ·

A wash solution for removal of unbound proteins, unreacted antisera, and excess stain from an electrophoresis gel plate and a method of using the wash solution. The wash solution contains one or more of Hexamethylindanopyran, Tetramethyl acetyloctahydronaphthalenes, Hexyl cinnamal, Butylphenyl methylpropional, d-Limonene and Linalool. Alternatively, the wash solution react with lipids and fats in the unbound proteins and/or unreacted antisera, and/or causes pores in the gel to expand yielding a more efficient removal of unbound protein and unbound antisera, and/or contains protease enzymes that digest proteins and an amylase enzyme to hydrolyze starches and sugars.

Wash for electrophoresis
12339248 · 2025-06-24 · ·

A wash solution for removal of unbound proteins, unreacted antisera, and excess stain from an electrophoresis gel plate and a method of using the wash solution. The wash solution contains one or more of Hexamethylindanopyran, Tetramethyl acetyloctahydronaphthalenes, Hexyl cinnamal, Butylphenyl methylpropional, d-Limonene and Linalool. Alternatively, the wash solution react with lipids and fats in the unbound proteins and/or unreacted antisera, and/or causes pores in the gel to expand yielding a more efficient removal of unbound protein and unbound antisera, and/or contains protease enzymes that digest proteins and an amylase enzyme to hydrolyze starches and sugars.

APTAMER BASED AFFINITY CAPTURE METHODS FOR THE SELECTIVE ENRICHMENT OF HUMAN IMMUNOGLOBULIN FC DOMAINS

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 M to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

APTAMER BASED AFFINITY CAPTURE METHODS FOR THE SELECTIVE ENRICHMENT OF HUMAN IMMUNOGLOBULIN FC DOMAINS

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 M to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

Assay for rapid detection of cerebrospinal fluid leaks

The invention encompasses methods and test strips for detecting the presence of cerebrospinal fluid (CSF) in a biological sample with a lateral flow device which uses lectin conjugates, anti-antigen conjugates, an immobilized serum line, and an immobilized anti-antigen line.

Assay for rapid detection of cerebrospinal fluid leaks

The invention encompasses methods and test strips for detecting the presence of cerebrospinal fluid (CSF) in a biological sample with a lateral flow device which uses lectin conjugates, anti-antigen conjugates, an immobilized serum line, and an immobilized anti-antigen line.

METHOD FOR IMMUNODETECTION USING ANTIBODY COCKTAIL

A method of detection of one or more antigens using a cocktail of one or more primary and secondary antibodies in a single step using a non-conventional Western blot protocol. Various antibody cocktails that can be used in the immunodetection methods.

METHOD FOR IMMUNODETECTION USING ANTIBODY COCKTAIL

A method of detection of one or more antigens using a cocktail of one or more primary and secondary antibodies in a single step using a non-conventional Western blot protocol. Various antibody cocktails that can be used in the immunodetection methods.

Multiplex competition assay for profiling binding epitopes of affinity agents for clinical diagnostics use

Some embodiments of the systems and methods provided herein relate to an assay. Some such embodiments include multiplex affinity probes and an antigen probe. multiplex affinity probes and an antigen probe Some embodiments include contacting a biological sample with the probes, wherein target binding agents such as antibodies in the biological sample compete away the multiplex affinity probes from binding to the antigen probe. Some such embodiments include detecting a decrease in binding of the multiplex affinity probes to the antigen probe, thereby indicating the presence or an amount of the target binding agents in the biological sample.

Method and system of microfluidic immunoassay using magnetic beads

A microfluidic Western blot method and system including a microfluidic western blot method for immunoassay of proteins, the method including introducing a sample including the proteins onto a chip; electrophoretically separating the proteins; binding the separated proteins to beads to form protein-attached beads, the beads being magnetic; flowing the protein-attached beads into a magnetic holding region; applying a magnetic field to the magnetic holding region to fix the protein-attached beads in place within the magnetic holding region; binding primary antibodies to target proteins on the protein-attached beads; binding secondary antibodies to the bound primary antibodies; and detecting the bound secondary antibodies.