Abstract: Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples.

Abstract: Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples.

Abstract: Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples.

Abstract: Methods and devices for purifying, detecting, and collecting analytes fractionated based on pI, separating analytes via electrophoresis and pI, and purifying a target molecule using pI focusing and subsequent crystallization are provided.

Abstract: Apparatuses and methods for controlling ionic strength and/or pH of a solution are provided.

Abstract: Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples.

Abstract: Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples.

Abstract: Apparatuses and methods for controlling ionic strength and/or pH of a solution are provided.

Abstract: Apparatuses and methods for purifying proteins and other target molecules based on pI are provided.

Abstract: Methods and devices for purification of different cell components from the same sample are provided.

Abstract: Methods and devices for purifying, detecting, and collecting analytes fractionated based on pI, separating analytes via electrophoresis and pI, and purifying a target molecule using pI focusing and subsequent crystallization are provided.

Abstract: Phosphorylated peptides are extracted from digests of biological liquids and other peptide mixtures by fractionation on ceramic hydroxyapatite. The ceramic hydroxyapatite is readily usable in a centrifuge, allowing for rapid fractionations of a large number of small volume samples, and accordingly high throughput.

Abstract: Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples.

Abstract: Apparatuses and methods for purifying proteins and other target molecules based on pI are provided.

Abstract: Apparatuses and methods for controlling ionic strength and/or pH of a solution are provided.

Abstract: Phosphorylated peptides are extracted from digests of biological liquids and other peptide mixtures by fractionation on ceramic hydroxyapatite. The ceramic hydroxyapatite is readily usable in a centrifuge, allowing for rapid fractionations of a large number of small volume samples, and accordingly high throughput.

Abstract: Microfluidic devices are provided where barriers are introduced between different compartments of the device to prevent fluid flow between the two compartments. Different materials and methods are employed for the introduction and removal of the barriers, including reversible gel particle expansion, reversible gellation, in situ polymerization, magnetic beads, and the like. In this way mixing of agents may be temporally controlled during the operation of the device, where the barriers may be used in a passive manner or as an active agent involved in the operation being performed in the device.

Abstract: Process for the selective separation of electrically charged target molecules in an analytical mixture by means of capillary affinity gel electrophoresis, using a capillary tube which is at least partly filled with a polymer gel, whereby receptors for target molecules are covalently bound to the polymer, and an electric field of at least 50 volts/cm is applied, characterized in that (a) the capillary tube is charged with the analytical mixture, (b) in a first separation stage the target molecules in the analytical mixture are bound to the receptors and the remaining components are eluted, optionally while splitting open, and (c) in a second stage of the process the elution conditions are changed, optionally in stages, so that the affinity of the target molecules for the receptor is eliminated and the target molecules are eluted and detected, optionally whilst splitting open.

Abstract: An improved microstructure for micro-scale fluid handling, processing and investigation comprises a support element and a microstructured element. The support element has a substantially even support face. The microstructured element has a microstructured face provided both with substantially even portions and with recessed portions. The even portions are substantially coplanar to a common even surface. The recessed portions are defined between the even portions adjacent thereto and recessed from the common even surface. The support face is located substantially adjacent to the microstructured face and cooperates with the recessed portions thereof to define a microchannel system. At least the microstructured element is made and formed of poly(dimethylsiloxane) polymer by applying a prepolymer or a precursor thereof onto a corresponding master element, and then curing the material.

Abstract: A device for combined bioaffinity assay and electrophoretic separation is provided, which comprises a capillary system having two stages, a first stage in which bioaffinity interactions of analyte molecules and molecular recognition elements are performed, and a second stage, in which electrophoretic separation of the analyte molecules and subsequent detection of the separated species is accomplished. Within the first capillary stage the molecular recognition elements are attached and immobilized to the inside capillary wall, for example, by adsorption or by covalent binding to the capillary material. The method for combined bioaffinity assay and electrophoretic separation comprises flowing an analyte through a capillary system having two stages. In a first capillary stage the analyte molecules are captured by respective molecular recognition elements present in that stage.