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Large scale protein purification - Yellow and cyan fluorescent protein (Sep/16/2005 )

Hi,

Has anyone purified fluorescent proteins before? I have cells that are overexpressing CFP (cyan fp) and cells overexpressing YFP (yellow fp). I have been purifying them on a small scale using the hydrophobicity column from Bio-Rad. However, the purification will only give me 750 ul and I'm looking to get lots more than that - somewhere between 100-500 ml. It's just absurd to repeat the purification with multiple columns..I would have to do hundreds of them!! Anyone has any experience with fluorescent protein purification? I would be delighted to get some suggestions.

-lilsquirr3l-

The following link might help.

For volume <70ml
http://www.millipore.com/markets/bioscienc...proteinresearch

For volume <500ml
http://www.millipore.com/catalogue.nsf/docs/C1975

-sallylyc-

Thanks a whole bunch! But we're looking on something that does not require anymore new equipment...something that costs less. But the site definitely gave me some idea. Thanks!

-lilsquirr3l-

In one of my grad school rotations I purified both CFP and YFP with his-tags using a denatured protocol - lyse the cells, add GuHCl up to ~ 6M, run it through a Ni affinity column, elute and dialyse. These particular proteins are stable enough to fold on their own without chaperones.

To convert to a system like this, you'd need to reclone them into vectors that express his-tags (minimal cost, assuming you have the enzymes - you can request the vector from a published source), some Ni-NTA agarose resin (fairly cheap as reagents go, but not a minor cost), and a whole bunch of Gu-HCl (something like 30$/kg, less if you order more of course).

Out of curiosity, why are you looking for 100-500 ml of protein? Is that a typo? Usually you look for protein in the "mg/ml" or "micromolar" range, then dilute to however much you need. Are you just making a huge stock, or is it a new application?

-aludlam-

QUOTE (aludlam @ Sep 20 2005, 09:56 AM)
In one of my grad school rotations I purified both CFP and YFP with his-tags using a denatured protocol - lyse the cells, add GuHCl up to ~ 6M, run it through a Ni affinity column, elute and dialyse. These particular proteins are stable enough to fold on their own without chaperones.

To convert to a system like this, you'd need to reclone them into vectors that express his-tags (minimal cost, assuming you have the enzymes - you can request the vector from a published source), some Ni-NTA agarose resin (fairly cheap as reagents go, but not a minor cost), and a whole bunch of Gu-HCl (something like 30$/kg, less if you order more of course).

Out of curiosity, why are you looking for 100-500 ml of protein? Is that a typo? Usually you look for protein in the "mg/ml" or "micromolar" range, then dilute to however much you need. Are you just making a huge stock, or is it a new application?


Thanks! But it would be a lot better if I don't have to go through the cloning steps again since protein purification is not my main study. Furthermore, we don't have any vectors with his-tag and we don't do any protein purification stuff in our lab either.

I am trying to measure these two proteins in different bacterial species as a measure of ribosomal translation efficiency. However, I need to have a standard for these two proteins to be able to get an approximation of the concentration. Unfortunately, I've tried looking around for companies selling purified CFP and YFP but I couldn't find any. Clontech sells GFP but that would have a different excitation and emission wavelength, which will just complicate the calculations later. So I have to purify it myself and get a large amount of it so that I don't have to do it everytime I need a standard.

-lilsquirr3l-