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A long incubation was required as the denaturing buffer was excluded from the reaction to avoid conformational changes that might abrogate virion binding.
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The colonies on the edges of the plates, the WT buffer, were excluded from further analysis as the sizes of these colonies are biased by 'edge effects' (the decreased competition resulting from being on the edge).
Kinase activity assays were performed in duplicate in gel filtration buffer (BME was excluded from the buffer for chemically modified variants that contained dehydroalanine) using a LabChip EZ Reader II system (Caliper Life Sciences) with 1.5 μM fluorescein-labeled Caliper Peptide 21 (Flu-LRRASLG) as the substrate and 12-point 2-fold serial dilutions of ATP.
When the temperature was between 50°C and 70°C minor variations in fluorescence were observed at acidic pH; such variations were eliminated when magnesium chloride was excluded from the buffer.
Briefly, fcPsV were produced by following the standard PsV production protocol [ 39, 40] with the following modifications: (1) instead of 293TT cells, 293TTF cells were used; (2) ammonium sulfate was excluded from the maturation buffer; (3) the concentration of CaCl2 in the maturation buffer was increased to 5 mM; and (4) maturation time was increased from 24 hours to 48 hours.
Triton X-100 was excluded from purification buffers due to its interference in mass spectrometry analysis of the protein.
For negative control DAB was excluded from the reaction buffer.
Primary antibodies were incubated in blocking solution for 2 h at room temperature at the following concentrations: PAX6 (Covance) 1 300, PAX2 (Lifespan Biosciences) 1 100, and Laminin (Abcam) 1 200; Triton X-100 was excluded from the blocking buffer for incubations with anti-Laminin.
A 3km buffer zone around each of the villages in the swamp forests was excluded from the survey zone.
He was excluded from meetings.
No sample was excluded from this work.
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