Dear Kostas,
MBP by itself is a monomer. In most of our cases using it as a fusion tag, the yield of a target protein increases drastically (i.e. 5 to >20 folds more). However, we have seen in a couple of cases that the target proteins strongly interact with the MBP tag, which causes oligomerization of the fusion protein. To check whether you have encountered a similar issue, you can try to cut the tag off and check whether your protein still sticks to MBP. Good luck, Gang From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Konstantinos Paraskevopoulos Sent: Wednesday, July 24, 2013 3:07 PM To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] Maltose binding protein as a tag Dear all, I would like to ask if someone has experience with maltose binding protein (MBP) as a tag. My protein fused to MBP seems to form oligomers that I find difficult to prevent and I was wondering if mbp behaves similar to gst and may also be prone to dimerisation/oligomerisation Many thanks in advance Kostas Paraskevopoulos Research fellow University of edinburgh
