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Capillary electrophoresis (CE) is a family of electrokinetic separation methods performed in submillimeter diameter capillaries and in micro- and nanofluidic channels.Very often, CE refers to capillary zone electrophoresis (CZE), but other electrophoretic techniques including capillary gel electrophoresis (CGE), capillary isoelectric focusing (CIEF), capillary isotachophoresis and micellar ...
The data is plotted with time, shown via base pairs (bps), on the x-axis and fluorescence intensity on the y-axis. Such plots are often achieved using an instrument such as an automated DNA sequencer paired with capillary electrophoresis (CE). Such electropherograms may be used to determine DNA sequence genotypes, or genotypes that are based on ...
Electrophoresis is a laboratory technique in which the blood serum (the fluid portion of the blood after the blood has clotted) is applied to either an acetate membrane soaked in a liquid buffer, [3] or to a buffered agarose gel matrix, or into liquid in a capillary tube, and exposed to an electric current to separate the serum protein ...
Oligoclonal bands (OCBs) are bands of immunoglobulins that are seen when a patient's blood serum, or cerebrospinal fluid (CSF) is analyzed. They are used in the diagnosis of various neurological and blood diseases. Oligoclonal bands are present in the CSF of more than 95% of patients with clinically definite multiple sclerosis. [1]
Individual instruments, of a particular model type, have also been known to differ in performance (e.g. differences among various ABI 310 units, all of the same model). Capillary electrophoresis instruments generally provide better resolution compared gel-based systems, as well having better sensitivity.
[1] [2] Capillary electrochromatography is a combination of two analytical techniques, high-performance liquid chromatography and capillary electrophoresis. Capillary electrophoresis aims to separate analytes on the basis of their mass-to-charge ratio by passing a high voltage across ends of a capillary tube , which is filled with the analyte.
The original interface between capillary zone electrophoresis and mass spectrometry was developed in 1987 [9] by Richard D. Smith and coworkers at Pacific Northwest National Laboratory, and who also later were involved in development of interfaces with other CE variants, including capillary isotachophoresis and capillary isoelectric focusing.
Affinity capillary electrophoresis takes the advantages of capillary electrophoresis and applies them to the study of protein interactions. [16] ACE is advantageous because it has a high separation efficiency, has a shorter analysis time, can be run at physiological pH, and involves low consumption of ligand/molecules.