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  2. Acid guanidinium thiocyanate-phenol-chloroform extraction

    en.wikipedia.org/wiki/Acid_guanidinium...

    RNA partitions in the aqueous phase, while proteins and DNA partition into the organic/interphase (left). The RNA is then precipitated in an alcohol (right). Acid guanidinium thiocyanate-phenol-chloroform extraction (abbreviated AGPC) is a liquid–liquid extraction technique in biochemistry and molecular biology.

  3. Protein purification - Wikipedia

    en.wikipedia.org/wiki/Protein_purification

    The protein manufacturing cost remains high and there is a growing demand to develop cost efficient and rapid protein purification methods. Understanding the different protein purification methods and optimizing the downstream processing is critical to minimize production costs while maintaining the quality of acceptable standards of homogeneity. [2]

  4. Cell disruption - Wikipedia

    en.wikipedia.org/wiki/Cell_disruption

    Many proteins are extremely temperature-sensitive, and in many cases can start to denature at temperatures of only 4 degrees Celsius. Within the microchannels, temperatures exceed 4 degrees Celsius, but the machine is designed to cool quickly so that the time the cells are exposed to elevated temperatures is extremely short ( residence time 25 ...

  5. Phenol–chloroform extraction - Wikipedia

    en.wikipedia.org/wiki/Phenol–chloroform_extraction

    Aqueous samples, lysed cells, or homogenised tissue are mixed with equal volumes of a phenol:chloroform mixture. This mixture is then centrifuged. Because the phenol:chloroform mixture is immiscible with water, the centrifuge will cause two distinct phases to form: an upper aqueous phase, and a lower organic phase.

  6. Protein methods - Wikipedia

    en.wikipedia.org/wiki/Protein_methods

    Protein purification is a critical process in molecular biology and biochemistry, aimed at isolating a specific protein from a complex mixture, such as cell lysates or tissue extracts. [9] The goal is to obtain the protein in a pure form that retains its biological activity for further study, including functional assays, structural analysis, or ...

  7. Tandem affinity purification - Wikipedia

    en.wikipedia.org/wiki/Tandem_Affinity_Purification

    Tandem affinity purification (TAP) is an immunoprecipitation-based purification technique for studying proteinprotein interactions. The goal is to extract from a cell only the protein of interest, in complex with any other proteins it interacted with. TAP uses two types of agarose beads that bind to the protein of interest and that can be ...

  8. Lysis buffer - Wikipedia

    en.wikipedia.org/wiki/Lysis_buffer

    RIPA buffer is a commonly used lysis buffer for immunoprecipitation and general protein extraction from cells and tissues. The buffer can be stored without vanadate at 4 °C for up to 1 year. [10] RIPA buffer releases proteins from cells as well as disrupts most weak interactions between proteins. [9] Recipe: [10] 1% (w/w) Nonidet P-40 (NP-40)

  9. Ammonium sulfate precipitation - Wikipedia

    en.wikipedia.org/wiki/Ammonium_sulfate_precipitation

    Proteins differ markedly in their solubilities at high ionic strength, therefore, "salting out" is a very useful procedure to assist in the purification of the desired protein. Ammonium sulfate is commonly used for precipitation because of its high solubility, additionally, it forms two ions high in the Hofmeister series .