Regarding purification look up for his-tagging and nickel column purification: it is not too difficult and if you get the solutions needed it would say it is DIYable.
The classical way uses a column and a detector for the pH fraction with your protein. You could hack a column, however keep in mind that you can also perform the whole purification procedure in a falcon tube and just using a centrifuge (and usually it gives better results).
As long as you are purifying the same protein you can re-use the same sephadex beads (when you read the protocol you'll understand what they are).
On Tuesday, 3 May 2016 12:00:25 UTC+2, Strat-o wrote:
The classical way uses a column and a detector for the pH fraction with your protein. You could hack a column, however keep in mind that you can also perform the whole purification procedure in a falcon tube and just using a centrifuge (and usually it gives better results).
As long as you are purifying the same protein you can re-use the same sephadex beads (when you read the protocol you'll understand what they are).
On Tuesday, 3 May 2016 12:00:25 UTC+2, Strat-o wrote:
Starting to develop a keen interest in this topic. First post.Let's say I have a viable bacterium (with my protein of interest inserted into a plasmid) and i inoculate a suitable growth media with my e. coli.1. Do I need to anything special to ensure that my protein of interest gets expressed?2. After the growth phase has run its course, how to i extract my protein of interest? (I assume there's not just one way, just interested in approaches to purification)Thanks!
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