SUMO fusion technology for difficult-to-express proteins.
SUMO fusion technology for difficult-to-express proteins.
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DOI：
10.1016/j.pep.2005.03.016
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发表时间：
2005-09
影响因子：
1.6
通讯作者：
Mattern MR
中科院分区：
文献类型：
--
作者：
Butt TR;Edavettal SC;Hall JP;Mattern MR
The demands of structural and functional genomics for large quantities of soluble, properly folded proteins in heterologous hosts have been aided by advancements in the field of protein production and purification. Escherichia coli, the preferred host for recombinant protein expression, presents many challenges which must be surmounted in order to over-express heterologous proteins. These challenges include the proteolytic degradation of target proteins, protein misfolding, poor solubility, and the necessity for good purification methodologies. Gene fusion technologies have been able to improve heterologous expression by overcoming many of these challenges. The ability of gene fusions to improve expression, solubility, purification, and decrease proteolytic degradation will be discussed in this review. The main disadvantage, cleaving the protein fusion, will also be addressed. Focus will be given to the newly described SUMO fusion system and the improvements that this technology has advanced over traditional gene fusion systems.
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影响因子：
5.6
作者：
Bayer, P;Arndt, A;Becker, J
通讯作者：
Becker, J
DOI：
10.1016/j.bbrc.2004.07.189
发表时间：
2004-09-24
影响因子：
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作者：
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通讯作者：
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影响因子：
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影响因子：
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作者：
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通讯作者：
Creighton, TE