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The gel is a regular SDS-PAGE (10%), the sample was prepared in a standard fashion (1x SDS loading buffer with BME, boiled for 10 min). The sample has been at -20C since arriving. There are no degradation products on the gel, as would be the case if storage or transportation was an issue. The two other bands are higher MW contaminants. The isocitrate DHase does appear to be active. Gel image is attached (first lane marker, second lane 1uL of sample, third lane 2uL of sample). Thanks.
Asked on May 16 2012
Thank you for your reply.
I was in touch with the supplying lab and they weren't sure why the higher band was being detected.They verified this protein with 15% SDS-PAGE and hadn't identified anyimpurities above 70kDa.
They wondered ifthis higher MW band maybe at approximately 97kDa? If so, it could correspond to its homodimer form. Can you identify the MW marker sizes?
If that's not the case, would you like a replacement protein? How would you like to proceed?
Answered on May 16 2012