A nanoscale protein-sensing platform with a non-equilibrium on-off switch that employs dielectrophoretic and hydrodynamic shear forces to overcome these thermodynamic limitations with irreversible kinetics. The detection sensitivity is achieved with complete association of the antibody-antigen-antibody (Ab-Ag-Ab) complex by precisely and rapidly assembling carbon nanotubes (CNT) across two parallel electrodes via sequential DC electrophoresis and dielectrophoresis (DEP), and with single-CNT electron tunneling conductance. The high selectivity is achieved with a critical hydrodynamic shear rate between the activated dissociation shear rates of target and non-target linkers of the aligned CNTs.

The present disclosure relates to the use of microfluidic devices and systems to generate dynamic molecular signatures based on the detection of various biocellular markers. In particular, the present disclosure involves generating a dynamic molecular signature or profile using the cells of a subject (e.g., circulating monocytes), for various diagnostic and prognostic purposes, such as characterizing a disease or non-disease state, or predicting drug responsiveness. The microfluidic systems and methods of the present disclosure can be used to rapidly assess a plurality of clinical characteristics, which will ultimately enhance therapeutic efficacy and facilitate disease risk stratification.

The present disclosure relates to the use of microfluidic devices and systems to generate dynamic molecular signatures based on the detection of various biocellular markers. In particular, the present disclosure involves generating a dynamic molecular signature or profile using the cells of a subject (e.g., circulating monocytes), for various diagnostic and prognostic purposes, such as characterizing a disease or non-disease state, or predicting drug responsiveness. The microfluidic systems and methods of the present disclosure can be used to rapidly assess a plurality of clinical characteristics, which will ultimately enhance therapeutic efficacy and facilitate disease risk stratification.

Electrophoretic separation methods and devices for detecting a distribution of analytes in a tissue sample are provided. The methods and devices find use in a variety of different electrophoretic separation applications, such as tissue projection electrophoretic separation of proteins from a tissue sample, where analytes in a tissue sample can be detected to produce a map of the distribution of the analytes in the tissue sample.

An electrophoretic device for detecting biomarkers in collected bodily fluid and methods of using the same.

An electrophoretic device for detecting biomarkers in collected bodily fluid and methods of using the same.

An ITP-based system and a method are provided. ITP is used to focus a sample of interest and deliver a high concentration target to a pre-functionalized surface comprising immobilized probes, thus enabling rapid reaction at the sensor site.

An ITP-based system and a method are provided. ITP is used to focus a sample of interest and deliver a high concentration target to a pre-functionalized surface comprising immobilized probes, thus enabling rapid reaction at the sensor site.

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.

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.