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What is another word for Isoelectric Focusing?

Pronunciation: [ˌa͡ɪsə͡ʊlˈɛktɹɪk fˈə͡ʊkəsɪŋ] (IPA)

Isoelectric focusing (IEF) is a powerful technique used in biochemistry and molecular biology for separating proteins based on their isoelectric point (pI). This method exploits the differences in the charges of proteins at specific pH levels. In IEF, an electric field is applied to a gel matrix with a pH gradient. As proteins move through the gradient, they migrate towards their pI, where they become electrically neutral and hence immobilized in the gel. IEF is also known as electrofocusing, electrofocalization, or isoelectrofocalization. By using these synonyms, scientists can easily communicate and exchange information about this valuable protein separation technique.
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What are the opposite words for Isoelectric Focusing?

Isoelectric focusing is a technique used to separate and purify proteins based on their isoelectric points. However, there are several antonyms or opposites for this technique that are employed in protein research. One such antonym is "native gel electrophoresis," which separates proteins based on their size and shape rather than their isoelectric points. Another antonym is "affinity chromatography," which separates proteins based on their specific interactions with ligands or substrates. Additionally, "ion-exchange chromatography" separates proteins based on their charge properties. These techniques are often used in combination with isoelectric focusing to achieve a more comprehensive protein separation and purification process.

What are the antonyms for Isoelectric focusing?

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