Lysate

The lysate is then filtered and placed on the ion-exchange column. ❋ Unknown (2005)

( "lysate") and GST-Plk1-PBD associated 53BP1 were analyzed by immunoblotting using anti-GFP antibody. ❋ Marcel A. T. M. Van Vugt Et Al. (2010)

Most striking was the finding that depletion of haem, and addition of GSSG or dsRNA all seemed to have similar effects on cell-free protein synthesis in the reticulocyte lysate, as though these disparate agents all acted in a similar manner. ❋ Unknown (2002)

One other thing I learned about during the studies on the inhibition of protein synthesis by dsRNA was that micrococcal nuclease, which requires Ca2+ for activity, did not inhibit protein synthesis in the reticulocyte lysate provided no Ca2+ was present. ❋ Unknown (2002)

I also discovered that simple gel-filtration of the lysate caused a drastic fall in its activity. ❋ Unknown (2002)

By 1977, the outlines of all this were pretty clear, and we had a very good understanding of the reticulocyte lysate and its properties. ❋ Unknown (2002)

The micrococcal nuclease calcium dependence was put to good use by Hugh Pelham, a graduate student in the lab, who developed the use of nuclease treatment of the lysate to assay heterologous mRNAs. ❋ Unknown (2002)

Lower panels are immunoblots showing equal loading of cardiac lysate to each reaction. ❋ Parveen Sharma Et Al. (2010)

Plasma membrane and total cell lysate proteins were resolved by SDS-PAGE, blotted on PVDF membrane and probed with anti-GLUT4 antibody. ❋ Alfredo Csibi Et Al. (2010)

Peptide columns were incubated either with 400 µl RD-FUR cell lysate in non-denaturating RIPA buffer (approximately 1 mg of total protein) or with 5U of recombinant human furin (approximately 250 ng of pure enzyme, Alexis Corporation) in 100 µl ❋ Katarina Hajdin Et Al. (2010)

In the left panel, 3% of the lysate input used in the immunoprecipitations was subjected to western blot analysis using an anti-ubiquitin antiserum to show that general ubiquitination levels were similar in all genotypes. ❋ Angela C. Poole Et Al. (2010)

For each lysate, the total protein concentration was determined using the Bradford assay (Bio-Rad). ❋ Michel V. L�vesque Et Al. (2010)

The resulting lysate was subjected to centrifugation at 12,000 ❋ Angela C. Poole Et Al. (2010)

To allow antibody-protein complex formation, the cleared lysate was incubated at 4°C under continuous rotation with antibody in binding buffer (140 mM NaCl, 8 mM NaPO4, 2 mM KPO4, 14 mM KCl pH 7.4) and 0.1% ❋ Parveen Sharma Et Al. (2010)

The lysate was then cleared by centrifugation for 15 min at 2600 rpm at 4°C. ❋ Parveen Sharma Et Al. (2010)

A: Blots of the plasma membrane or total cell lysate proteins were probed with anti-GLUT4 antibody. ❋ Alfredo Csibi Et Al. (2010)

Protein G Sepharose (GE Healthcare, Piscataway, NJ) beads were then added to the lysate for 3 hours, collected by low-speed centrifugation, washed three times in lysis buffer and boiled in 2X SDS-PAGE sample buffer with 2% beta-mercaptoethanol for 10 minutes to release immunoprecipitated dMfn. ❋ Angela C. Poole Et Al. (2010)

Three percent of the total amount of lysate used for the immunoprecipitations as well as the Parkin immunoprecipitates were subjected to western blot analysis with the anti-dMfn antiserum. ❋ Angela C. Poole Et Al. (2010)

Limulus amebocyte lysate (LAL) reaction kit (E-Toxate; Sigma, St Louis, MO). ❋ Neelkamal Chaudhary Et Al. (2010)