pBAD-Thio-TRP36

Protein Expression Prokaryotic cells - E. coli TRP36 Ehrlichia canis

Experiment
Protein Expression Prokaryotic cells - E. coli TRP36 Ehrlichia canis
Product
pBAD-Thio-TRP36 from Nádia Regina Pereira Almosny, Departamento de Patologia Clínic
Manufacturer
Nádia Regina Pereira Almosny, Departamento de Patologia Clínic

Protocol tips

Protocol tips
Recombinant plasmids were first screened for the TRP36-fusion protein expression using L- (+)-arabinose as the inductor. After a small-scale experiment to determine the optimal concentration of the sugar, one positive clone was grown overnight in LB medium containing 100 μg/mL ampicillin at 37 °C under shaking (250 rpm).

Publication protocol

Recombinant plasmids were first screened for the TRP36-fusion protein expression using L- (+)-arabinose as the inductor. After a small-scale experiment to determine the optimal concentration of the sugar, one positive clone was grown overnight in LB medium containing 100 μg/mL ampicillin at 37 °C under shaking (250 rpm). This overnight culture was inoculated into 500 mL of LB medium in a 1 L culture flask for the large-scale expression experiment. The culture was maintained at 37 °C under shaking until an OD550 of 0.5. L-arabinose was then added to a final concentration of 0.002%, and the culture was grown for 4 h at 25 ºC under shaking. After reaching the corresponding OD, cells were harvested by centrifugation (9,500 x g) for 20 min at 4 ºC. The pellet was suspended in phosphate buffer saline (PBS) at pH 7.4, and a 100 μL sample was analyzed by 12% SDS-PAGE under denaturing and reducing conditions, as described by Laemmli (1970). The remainder of the preparation was centrifuged, and the pellet was resuspended in 10 mL of ice-cold binding buffer (20 mM sodium phosphate buffer, pH 7.8, containing 500 mM NaCl and 10 mM imidazole) plus lysozyme (1 mg/ mL), mixed with microglass beads (0.1 mm) v/v, and subjected to three 10 s pulses at 10 s intervals in the Bead Beater (model 1107900, Biospec, Bartlesville, USA). After glass bead sedimentation, the supernatant was transferred to a Falcon tube to which DNase and RNase were added to a final concentration of 5 and 10 μg/mL, respectively. The mixture was centrifuged to pellet the debris and the microbeads, and the supernatant was stored for the future isolation of the TRP36-fusion protein.

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