Affinity purification of MLL3/MLL4 histone H3K4 methyltransferase complex.
Affinity purification of MLL3/MLL4 histone H3K4 methyltransferase complex.
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DOI:
10.1007/978-1-61779-376-9_30
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发表时间:
2012
期刊:
影响因子:
--
通讯作者:
Ge, Kai
中科院分区:
文献类型:
--
作者:
Cho, Young-Wook;Hong, SunHwa;Ge, Kai
Methylation on histone H3 lysine 4 (H3K4) correlates with actively transcribed genes. In mammalian cells, there exist multiple Set1-like histone H3K4 methyltransferase complexes, which have overlapping but distinct subunit compositions. Developing methods to isolate each of these histone H3K4 methyltransferase complexes would help understand the molecular mechanisms by which histone H3K4 methylation regulates mammalian gene expression. In this chapter, we provide a one-step affinity purification protocol on isolation of the MLL3/MLL4 histone H3K4 methyltransferase complex using FLAG-tagged PA1, a unique subunit of the MLL3/MLL4 complex.
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DOI:
10.1073/pnas.0707292104
发表时间:
2007-11-20
影响因子:
11.1
作者:
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通讯作者:
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