Hi Irit and everyone,

I heard BSA helps if the sample has very low concentration. I just wonder if 
the high BSA concentration would affect the later SDS-PAGE. Let say if you need 
to add BSA to 1mg/mL in 1mL sample. Finally, need to add all the sample for 
running SDS-PAGE in one well. So there is at least 1 mg of total proteins (Or 1 
mg BSA plus negligible amount of proteins from the original unconcentrated 
sample).
There are two problems I may concern. First, whether the lump formed by high 
concentration of BSA can be dissolved in sample buffer. Second, whether sample 
with such a high protein concentration would affect the resolution of the 
SDS-PAGE, esp for protein with small molecular weight. I tried to load 250micro 
gram total protein extracted from brain lysate and resolve it by SDS-PAGE, 
however, the resolution is very bad, esp at small molecular weight. My target 
protein is 4kD and I used 16.5% Tricine gel. The reference for this experiment 
was mentioned in Lesne S. et al., 2006, Nature, v440, 352-357 and its 
supplementary methods. But I never get it works.

Best,
Stan





________________________________
From: Irit Rappley <[email protected]>
To: Nikola Wenta <[email protected]>
Cc: "[email protected]" <[email protected]>
Sent: Fri, March 12, 2010 2:53:50 AM
Subject: Re: Protein precipitation - acetone?

Some people add 1 mg/mL BSA to their sample in order to get the total protein 
concentration high enough for precipitation. Of course, then you're left with 
lots of BSA in your precipitate too....



On Mar 11, 2010, at 9:27 AM, Nikola Wenta wrote:

> Hi Iraz!
> I don't have any clue about acetone precipitation of proteins, but generally, 
> precipitation with saturated Ammonium sulfate solution provides a good means 
> to concentrate proteins and to get them into a save state for short-term 
> storage. Unfortunatelly, you would already need the protein solution to be at 
> > 1 mg/ml in order to get it to precipitate. Thus, in your case this method 
> doesn't seem suitable. You could also try to concentrate the protein with 
> Centricons, but you would rather loose protein to the membrane than 
> concentrate your solution as it is already too diluted. Why not loading 
> maximum volume into biggest possible pockets on a gel with maximum thick 
> spacers? Additionally you could use a acrylamide percentage that "compresses" 
> your protein band, giving you a better signals in WB.
> Best, Niko
> 
> -----Ursprüngliche Nachricht-----
> Von: [email protected] im Auftrag von 
> [email protected]
> Gesendet: Do 11.03.2010 17:03
> An: [email protected]
> Betreff: Methods Digest, Vol 58, Issue 7
> 
> Message: 8
> Date: Thu, 11 Mar 2010 16:56:05 +0100
> From: "Iraz Toprak Aydin" <[email protected]>
> Subject: Protein precipitation - acetone?
> To: <[email protected]>
> Message-ID: <004401cac133$5b7c0df0$127429...@[email protected]>
> Content-Type: text/plain;    charset="us-ascii"
> 
> Dear all,
> 
> 
> 
> I have to do a western blot, but my protein concentration is very low, and I
> have to run a mini gel. So I was thinking of precipitation the proteins. I
> have never done this before. Does acetone have a bad effect on the blotting?
> Are there any points that I should be careful about?
> 
> 
> 
> Thanks in advance...
> 
> 
> 
> Iraz Toprak Aydin
> 
> 
> 
> EPFL SV ISREC, Station 19
> 
> Batiment SV, SV 2540
> 
> CH-1015 Lausanne
> 
> Switzerland
> 
> 
> 
> Tel: +41 21 693 07 36
> 
> 
> 
> e-mail:   <mailto:[email protected]> [email protected]
> 
> 
> 
> 
> 
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Irit Rappley, PhD
The Scripps Research Institute
BCC-265
10550 N Torrey Pines Rd.
La Jolla, CA 92037

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