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Protein purification encompasses numerous methods for the isolation of a native or recombinant protein from whole cells with minimal to no contamination. The generic steps for protein purification are: 1) extraction of proteins through cell lysis, 2) precipitation of all proteins in a salt buffer, 3) collection of the precipitated proteins through ultracentrifugation, 4) purification of the desired protein, 5) removal of residual salts, and 6) refolding, if the proteins are denatured (unfolded) during purification. Each step is modified based on the type of protein being purified and the method of purification. Methods for purification include chromatography methods such as size-exclusion and high performance liquid chromatography (HPLC), protein tagging methods that involve the addition of an affinity tag to a protein and then isolation over a binding column (such as His-tagging and isolation on a nickel column), and binding methods that involve isolating the desired protein by immobilizing a substrate of that protein on a membrane or column. Considerations when selecting a method include the amount of purified protein desired, level of purity desired, if the protein can be denatured or should be purified in its native form, and the number of purification steps desired. Protein purification has several applications spanning the study of protein function, antibody generation, and drug manufacturing. Insulin, human growth hormone, Lactaid, and Botox are examples of drugs that are purified proteins. (Credit: Brooke Anderson-White)
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