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Updated: Aug 19, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
An easy approach for the purification of native TFIIH
Enrique Castaño1, Ruben Dario Flores, Luis Carlos Rodriguez Zapata
1Unidad de Bioquímica y Biología Molecular de Plantas, Centro de Investigación Científica de Yucatán, Calle 43 No. 130, Col. Chuburná de Hidalgo, CP 97200, Mérida, Yucatán, México. enriquec@cicy.mx
Abstract:
Transcriptional regulation depends on the appropriate set of positive and negative regulating signals in order to provide the correct gene expression. In vitro studies in eukaryotic gene expression over the last few years have provided a wealth of information about new factors involved in the regulation of genes. However, the dissection of this mechanism requires the addition of well-characterized general transcription factors; with the exception of TFIID and TFIIH, all others can easily be expressed in a recombinant form. Here we provide a simple methodology to obtain partially purified transcriptionally active TFIIH free from other general transcription factors and active in transcription.

