TWO DIMENSIONAL IMMUNOELECTROPHORESIS Meaning and
Definition
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Two Dimensional Immunoelectrophoresis is a laboratory technique used to separate and identify proteins based on their charge and size using immunological methods. It involves the combination of two electrophoretic techniques: immunoelectrophoresis and two-dimensional gel electrophoresis.
In the first dimension, proteins are separated based on their charge using a technique called isoelectric focusing (IEF). A mixture of proteins is first applied to a gel with a pH gradient. An electric field is then applied across the gel, and proteins migrate towards the pH region that matches their isoelectric point (pI), the pH at which they have no net charge. This separation in the first dimension allows for the resolution of proteins with similar pI values.
In the second dimension, proteins are further separated based on their molecular weight using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The proteins from the first dimension are then separated in a second gel using SDS-PAGE, a technique that cancels out the effect of charge and allows separation solely based on size.
The separated proteins can then be visualized using staining methods or immunoblotting techniques, such as Western blotting, to identify specific proteins of interest based on their interaction with antibodies.
Overall, Two Dimensional Immunoelectrophoresis is a powerful technique that provides high-resolution separation of proteins based on their charge and molecular weight, allowing for the identification and characterization of protein mixtures in various research and diagnostic applications.
Common Misspellings for TWO DIMENSIONAL IMMUNOELECTROPHORESIS
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