The structural and functional genomics demands for large amounts of correctly folded soluble proteins in heterologous hosts have been aided by advances in the field of protein production and purification. Escherichia coli, the preferred host for recombinant protein expression, presents many challenges that must be overcome in order to overexpress heterologous proteins. These challenges include proteolytic degradation of target proteins, protein misfolding, poor solubility, and the need for good purification methodologies.
Gene fusion technologies have been able to enhance heterologous expression by overcoming many of these challenges. In this review, the ability of gene fusions to improve expression, solubility, purification, and decrease proteolytic degradation will be discussed. The main disadvantage, the cleavage of fusion proteins, will also be addressed. Attention will be given to the recently described N-terminal 10xHis-SUMO-tagged Recombinant fusion system and the improvements this technology has advanced over traditional gene fusion systems.
Keywords: Protein expression, Gene fusion, Protein fusion, Ubiquitin, SUMO, Ubiquitin-like proteins
N-terminal 10xHis-SUMO-tag negative control
Full product name
For research use only
For research use only. It should not be used in diagnostic procedures.
Host: E. coli
Manufactured in an ISO 9001:2015 certified laboratory.
Small volumes of N-terminal 10xHis-SUMO-tag and C-terminal Myc-tag Negative Control vials may occasionally become trapped in the product vial seal during shipping and storage. If necessary, briefly spin the vial in a tabletop centrifuge to dislodge any liquid in the vial cap. Certain products may require dry ice shipping and an additional dry ice fee may apply.
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