m not able to sequence it with the specific primers it could be
due to its low concentration.
Please advise.
Thank you.
--
Dr. Anamika Singh
Post-Doctoral Fellow
Silberman Institute of Life Sciences
Hebrew University of Jerusalem, Israel
No: 054-294
the co-transformation of these constructs?
On Thu, 26 Nov 2020 at 11:59, Anamika Singh wrote:
> Hi all,
>
> I have two constructs having different ori, p15ori and M13 ori, different
> promoters araC and LacI, and different antibiotic resistance
> chloramphenicol and Ampicillin
Hi all,
I have two constructs having different ori, p15ori and M13 ori, different
promoters araC and LacI, and different antibiotic resistance
chloramphenicol and Ampicillin respectively. I would like to know
which *expressing
E. coli host cells* will be good for the co-transformation of these
con
.
--
Anamika Singh
Post-Doctoral Fellow
Silberman Institute of Life Sciences
Hebrew University of Jerusalem, Israel
No: 054-294-8036
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plus.
Our lab is located in the Department of Biological Chemistry in the Hebrew
University of Jerusalem, Jerusalem, Israel.
Please contact Julia Shifman: jshif...@mail.huji.ac.il
--
Dr. Anamika Singh
Post-Doctoral Fellow
Silberman Institute of Life Sciences
Hebrew University of Jerusalem
Hi All,
I am purifying the biotinylated protein (cloned into the pET28a vector)
using Avidin beads. Since I need the protein for SPR but when I used the
purified protein to interact with Streptavidin coated onto the SPR chip.
There was no signal. Can anybody tell me why is it so or how can I make
Dear All,
I am purifying the His-tagged proteins ( 21Kda) using buffer 20mM Tris,
150mM Nacl, and 5mM MgCl2 with 500mM imidazole. Earlier I was facing the
precipitation problem during dialysis but with the addition of 50mM L-Arg
somehow managed to overcome the precipitation issue. But this time I
Hi,
Is anyone has worked with STAT1 proteins?
I have cloned the SH2 domain of STAT1 protein into pet28a vector but there
was no expression so far or rather say inconsistent expression. Sometimes
the expression was in inclusion bodies. I have tried different methods to
pull out the protein from i
Dear All,
I want to get some help regarding crystallization for one of the protein I
am working. This is a recombinant protein of molecular weight of 17.5 kDa. I
am getting crystals shape like thin plates in 5 days, in different
conditions like bis tris pH 6.5-8, HEPES pH 6-8 with .1M nacl , .01M
