Tandem Affinity Purification and Mass Spectrometry (TAP-MS)for the Analysis of Protein Complexes

Tipo de material: Texto

TextoSeries ; Current Protocols in protein Science, 96, p. https://doi.org/10.1002/cpps.84, 2019Trabajos contenidos:

Adelmant, G
Garg, B. K
Tavares, M
Card, J. D
Marto, J. A

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Resumen: Affinity purification followed by mass spectrometry has become the technique of choice to identify binding partners in biochemical complexes isolated from a physiologic cellular context. In this report we detail our protocol for tandem affinity purification (TAP)primarily based on the use of the FLAG and HA peptide epitopes, with a particular emphasis on factors affecting yield and specificity, as well as steps to implement an automated version of the TAP procedure.

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Affinity purification followed by mass spectrometry has become the technique of choice to identify binding partners in biochemical complexes isolated from a physiologic cellular context. In this report we detail our protocol for tandem affinity purification (TAP)primarily based on the use of the FLAG and HA peptide epitopes, with a particular emphasis on factors affecting yield and specificity, as well as steps to implement an automated version of the TAP procedure.

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