Methods for analyzing raw electropherogram data are disclosed. Some methods includes extracting color data as a function of time or position from the raw electropherogram data, selecting from the electropherogram one or more peaks that contain color data for a first dye and substantially no color data from other dyes used in electrophoresis. The method also includes determining the color spectrum of the first dye, and using the color spectrum of the first dye to deconvolve the color data of the raw electropherogram data to separate the contributions of each of the dyes to the raw electropherogram data. Systems and apparatus for producing electropherograms are also disclosed.

The invention described herein relates to an improved method for analytical capillary gel electrophoresis (CGE) for complex biologic molecules. The methods for the improved CGE include steps for the partial reduction of the biologic analyte molecule for use as calibration standard and use such partially reduced calibration sample to obtain an improved calibration curve for CGE to be used with biologic analyte molecules.

CAE sample tank. An outlet end of the capillary array is connected to the array channel CL reaction tank, and is further connected to the CAE detection tank.

The present disclosure relates to a method for using chemical tags which have two or more sites for ionization to improve quantification and identification of components of interest from a complex mixture. This method relies on first selectively reacting one or more component in a sample with a chemical tag having two or more sites for ionization, followed by separation of components based on charge status, and finally characterization of each component to identify the same. Additionally disclosed are compounds useful as chemical tags in the disclosed methods.

An immunofixation electrophoresis applicator system and method deposits antisera in spaced apart locations on a substrate where the antisera is deposited as an elongated bead in a first direction and retained against migration in a direction transverse to said first direction at least by surface tension.

A system for assaying a biological sample for a presence of a target analyte includes an assaying device and a computer controller. The assaying device includes a housing, a receptacle disposed in the housing, and a source of activation energy. The receptacle is configured to accept an electrophoresis cell. The electrophoresis cell has a recess area configured to accept a chip configured to accept the biological sample. The chip includes a polymeric separation medium with activatable functional groups that covalently bond to the target analyte when activated. The source of activation energy is configured to supply activation energy to activate the activatable functional groups. The computer controller is operably coupled to the source of activation energy and is configured to activate the source of activation energy to direct an application of activation energy to the polymeric separation medium to activate the activatable functional groups.

The present disclosure relates to a method for using chemical tags which have two or more sites for ionization to improve quantification and identification of components of interest from a complex mixture. This method relies on first selectively reacting one or more component in a sample with a chemical tag having two or more sites for ionization, followed by separation of components based on charge status, and finally characterization of each component to identify the same. Additionally disclosed are compounds useful as chemical tags in the disclosed methods.

Devices for detecting an analyte in a sample suspected of containing the analyte, are provided. The devices include bio-functional, nanostructured, isoporous membranes (BNIM) integrated organic electrochemical transistor (OECT), herein BNIM-OECT, for the rapid and sensitive detection of the presence of an analyte of interest, in a sample, for example, a biological sample. The membrane (i.e., BNIM) is physically separated from the OECT channel therefore the electronic device can be used multiple times. The isoporous membrane is functionalized to include a binding partner for the analyte being detected. The BNIM-OECT can be used for disease detection, by functionalizing the BNIM-OECT with a binding partner to an analyte associated with the disease, applying a collected biological sample to the BNIM-OECT. A decrease in channel current as a result of analyte binding to its binding partner on the isoporous membrane indicates the presence of the analyte in the sample.

Disclosed are miniaturized electronic systems, devices and methods for biomarker analysis, which can be incorporated into blood collection tubes and other containers that enable the immediate isolation, concentration, analysis and storage of disease related biomarkers upon blood draw. In some aspects, a miniaturized electronic system includes a high-surface area folded or sandwiched electrokinetic microelectrode array chip device that allows both AC dielectrophoretic (DEP) and DC electrophoretic based separation and isolation and other processes to be used for the concentration and biomarkers.

The present disclosure provides a method for identifying a human growth hormone proteoform (hGHP) pattern biomarker. The method includes: collecting an hGH-secreting pituitary adenoma tissue sample and a normal pituitary tissue sample, and extracting tissue proteins, separately; conducting two-dimensional gel electrophoresis (2DGE), western blotting, and Coomassie brilliant blue (CBB) staining, and scanning visualized polyvinylidene fluoride (PVDF) membranes and 2D gels to obtain digital images; subjecting a corresponding protein in 2D gel spot to protein digestion with trypsin and purification, and conducting mass spectrometry identification and bioinformatics analysis to identify a GHP biomarker profile; and in combination with bioinformatics, using quantitative phosphoproteomics, quantitative ubiquitinomics, and quantitative acetylomics to identify post-translational modifications (PTMs) and splicing variations in GHP. The present disclosure can identify a change pattern of GHP between a GH-secreting pituitary adenoma tissue and a normal pituitary tissue. In total, 46 GHPs are identified in the GH-secreting pituitary adenoma tissue, and only 35 GHPs are identified in the normal pituitary tissue. Therefore, 11 GHPs are only present in the GH-secreting pituitary adenoma tissue.