Close

BmrA

An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Loading...
CONTACT US
USA:
Europe:
Germany:
Call us at:
USA:
UK:
Germany:
Fax:
Email:
Our customer service representatives are available 24 hours a day, 7 days a week. Contact Us
© 2024 Creative Biolabs. | Contact Us