Apologies for the off-topic post, but the position in my group may be of
interest to students who have skills in protein expression and purification
wanting careers in industry. Many of my former students, staff and
post-docs have moved to high paying jobs in biotech and biopharma.
The Bioexpress
Mohinder,
You could also try HPLC where you should get better results due to more
theoretical plates. One option would from Phenomenex.
10E6A Phase Information
--
- Molecular Weight Range: 60 K - 10,000 K
https://www.phenomenex.com/Products/HPLCDetail/phenogel
*D
Hi Liuqing,
I would not recommend SEC. SEC does not give that great of a separation
unless your contaminant is greatly different in size. Instead of SEC, you
might want to consider hydrophobic interactions chromatography (HIC). You
can add your ammonium sulfate directly to your eluted protein f
Hi Anamika,
I did a search and it looks like researchers are using either mammalian
cells or baculovirus to express this protein. I don't have experience with
this particular construct so could you tell me why you choose *E. coli*? I
run a protein expression facility and we typically use HEK or
We have had good luck with columns from Essential Life Solutions (
http://www.essential-life.net/). They are easy to work with and hold up
under pressure well.
Best,
David
--
David L. Blum, Ph.D.
Director, Bioexpression and Fermentation Facility
Department of Biochemistry and Molecular Biol
Hi Reza,
Are there certain requirements for the collection of the fractions you need
from the UC run or do you just want advice on any type of collector?
For just regular collectors, have you tried eBay? I have had success
purchasing used equipment from there. A quick search turned up an old
Ph
Hi Sundaram,
The binding capacity of this column is 40 mg/mL of resin so a 5mL column
will hold a maximum of 200 mg of protein. If you run your cleared lysate
on a gel you may be able to estimate how much protein there is. Our
facility purifies a range of different proteins for investigators and
Sanjit,
We routinely use Protein G coupled resins for purification of monoclonals
produced in the facility. On a structural level, antibodies typically
recognize 5 or more residues in a protein unless the immunogen, such as a
single amino acid in your case, is a hapten conjugated to a carrier
mol
since it is also a webpage. You can attach an unlimited number of files,
but we usually put in links to the files that are stored on our server.
Happy to talk in more detail if you want to contact me offline.
David Blum
Bioexpression and Fermentation Facility
University of Georgia
b...@uga.edu
Dear Jacob,
We have been using factor XA for several years for tag removal of the
proteins we express in the facility. Factor XA does not leave an overhang,
cutting after an IEGR sequence. It can be quite expensive though so we are
looking into methods to purify it from bovine plasma.
David
Jackie,
We grow cells routinely and freeze pellets after fermentation. In general,
proteins are fairly stable until you break cells so you are probably ok
unless your protein is very heat labile and it sat at room temperature for
hours. However as I mentioned, there is a kind of buffering from t
Dear Phoebe,
We have a constant systems homogenizer that we use routinely as a service
for researchers here at UGA. It is really easy to use and gets up to high
pressure (40k psi) so you can lyse plant cells or other difficult to lyse
cell types. You just pour/pump your resuspended cells, as low
The Bioexpression and Fermentation Facility (BFF) within the Department of
Biochemistry and Molecular Biology at the University of Georgia invites
applicants for a non-tenure track position at the Assistant or Associate
Research Scientist level.
Please visit our website (http://bff.uga.edu) for de
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