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  2. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    Affinity chromatography can be used in a number of applications, including nucleic acid purification, protein purification [9] from cell free extracts, and purification from blood. By using affinity chromatography, one can separate proteins that bind to a certain fragment from proteins that do not bind that specific fragment. [10]

  3. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    Proteins can coordinate metal ions on their surface and it is possible to separate proteins using chromatography by making use of the difference in their affinity to metal ions. This is termed as immobilized metal ion affinity chromatography (IMAC), as originally introduced in 1975 under the name metal chelate affinity chromatography. [3]

  4. Strep-tag - Wikipedia

    en.wikipedia.org/wiki/Strep-tag

    The Strep-tag system is a method which allows the purification and detection of proteins by affinity chromatography.The Strep-tag II is a synthetic peptide consisting of eight amino acids (Trp-Ser-His-Pro-Gln-Phe-Glu-Lys).

  5. Periodic counter-current chromatography - Wikipedia

    en.wikipedia.org/wiki/Periodic_counter-current...

    Periodic counter-current chromatography (PCC) is a method for running affinity chromatography in a quasi-continuous manner. Today, the process is mainly employed for the purification of antibodies in the biopharmaceutical industry [1] as well as in research and development. When purifying antibodies, protein A is used as affinity matrix ...

  6. FLAG-tag - Wikipedia

    en.wikipedia.org/wiki/FLAG-tag

    It is one of the most specific tags [2] and it is an artificial antigen to which specific, high affinity monoclonal antibodies have been developed and hence can be used for protein purification by affinity chromatography and also can be used for locating proteins within living cells.

  7. Biotinylation - Wikipedia

    en.wikipedia.org/wiki/Biotinylation

    The biotin tag can be used in affinity chromatography together with a column that has avidin (or streptavidin or neutravidin) bound to it, which is the natural ligand for biotin. However, harsh conditions (e.g., 6M GuHCl at pH 1.5) are needed to break the avidin/streptavidin - biotin interaction, which will most likely denature the protein ...

  8. Chromatography - Wikipedia

    en.wikipedia.org/wiki/Chromatography

    Chromatography, pronounced / ˌ k r oʊ m ə ˈ t ɒ ɡ r ə f i /, is derived from Greek χρῶμα chrōma, which means "color", and γράφειν gráphein, which means "to write".". The combination of these two terms was directly inherited from the invention of the technique first used to separate biological pigme

  9. Ion chromatography - Wikipedia

    en.wikipedia.org/wiki/Ion_chromatography

    Ion chromatography (or ion-exchange chromatography) is a form of chromatography that separates ions and ionizable polar molecules based on their affinity to the ion exchanger. [1] It works on almost any kind of charged molecule —including small inorganic anions, [ 2 ] large proteins , [ 3 ] small nucleotides , [ 4 ] and amino acids .

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