Purification of His6-tagged Protein Using Immobilized Metal Ion Affinity Chromatogrphy
8:49
His6-tag Removal Using TEV Protease and Size-excluson Chromatography of Tlp3-LBD
11:06
Results: Expression, Refolding, and Purification of Tlp3-LBD
12:41
Conclusion
副本
The overall goal of this procedure is to refold a chemoreceptor ligand binding domain from inclusion bodies and purify it for use in structural and functional studies. To establish what signals a bacterial chemoreceptor sends and how, one can use
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A procedure is presented for the refolding of the dCACHE periplasmic ligand binding domain of Campylobacter jejuni chemoreceptor Tlp3 from inclusion bodies and the purification to yield milligram quantities of protein.