Sentence examples for harvest buffer from inspiring English sources

Cellular proteins were solubilized in ice-cold harvest buffer containing 0.5% Nonidet P-40, 50 mM Tris-HCl (pH 8.0), and 10 µM PMSF following the treatments indicated.

Lysed cells were resuspended in lysis buffer (harvest buffer brought up to high salt concentration (0.5 M KCl) and containing 1 mM PMSF).

The cell pellet was washed with 5 mls of Harvest Buffer (20 mM Hepes pH 7.4, 2 mM MgOAc, 100 mM KOAc), pelleted again as before, resuspend in 1 mL of harvest buffer, transferred to an eppendorf, pelleted with brief (10 sec) spin, supernatant was aspirated off, and the pellet was lysed immediately (see below) or stored pellet at −20°C.

Beads were then washed with TEV buffer (harvest buffer without protease inhibitors), and incubated overnight at 4°C with purified GST-TEV (tobacco etch virus) protease to cleave off Cdc24.

44 hours after infection, supernatants were discarded, cells were washed with PBS, lysed for 10 min at room temperature in harvest buffer (50 mM MES/Tris pH 7.8/10% glycerol/0.1% triton X100/1 µM DTT) and frozen at −80°C.

Cells were washed once with harvest buffer (50 mM HEPES pH 7.5, 0.1 M KCl, 3 mM MgCl2⋅6H2O, 1 mM EGTA, 50 mM NaF, 120 mM β-glycerophosphate, 1 mM Na3VO4, and 1 mM DTT, supplemented with a protease inhibitor cocktail containing 0.5 mg/ml each of antipain, leupeptin, aprotinin, pepstatin, and chymostatin (Sigma)).

If seasonal ponds are an important resource on the management landscape and a high percentage of upland forest is in a recently cut condition at any given time, than use of harvest buffers around seasonal ponds may be an appropriate approach for mitigating short term alteration of pond plant communities.

After growth, the crystals were mounted into appropriately sized loops and transferred to a harvesting buffer (3.0 M sodium malonate, 10% glycerol v/v, pH 7.0) supplemented with a saturated amount of substrate prior to flash cooling in liquid N2.

Briefly, cells were harvested, washed with Harvesting Buffer (50 mM HEPES ph 6.6, 140 mM NaCl, 3 mM MgCl2), regenerated with 11- cis retinal chromophore, solubilized (in 1% n-dodecyl-β-D-maltopyranoside detergent (DM) with 20% (w/v) glycerol), and purified by batch immunoaffinity chromatography with the 1D4 monoclonal antibody [ 78].

Cells were resuspended in 1 ml harvesting buffer (0.125 M glycine, 1 mM EDTA, 1 mM PMSF in PBS), pelleted (3000 rpm, 4 °C, 10 min) and lysed in 100 μl lysis buffer (50 mM Tris HCl, pH 8.0, 1% SDS, 10 mM EDTA).

For isolation of the HemG-containing inclusion bodies the cell pellet was redissolved in 10 ml harvesting buffer 100 mM Tris HCl, pH 8.0, lysozyme 0.2 mg/ml incubated for 5 min at room temperature and disrupted by sonication (0.5 s pulse, 0.5 s pause, 70% amplitude; KE76; Sonoplus HD 2070).