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Samples were incubated at 100°C for 5 min in a sample buffer and then separated by SDS-PAGE (12% gels).
Immunoprecipitates were washed three times with same lysis buffer and then separated by SDS-PAGE.
The protein was mixed with 2× SDS loading buffer and then, separated by electrophoresis in a 12.5% acrylamide gel.
For SDS-PAGE analysis, the expressed target protein was lysed in loading buffer and then separated by SDS-PAGE, followed by staining with Coomassie brilliant blue R-250.
Cell lysates were released by heating samples at 95°C for 10 minutes in Laemmli cooking buffer and then separated by SDS (sodium dodecylsuldate -polyacrylamide gel electrophoresis.
Samples were boiled with loading buffer and then separated by SDS/PAGE (10% gel) prior to being transferred to a nitrocellulose membrane (Millipore).
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Table 1 Esterase activity of the precipitated alpha chymotrypsin after redissolving them back in the aqueous buffer Enzyme preparation % Activity recovered Straight from the bottle - EPRP 97 ECCN 1 93.2 ECCN 2 91.6 ECCN 3 94.9 ECCN 4 92.4 ECCN 5 90.7 The EPRP and ECCNs were suspended back in 50 mM phosphate buffer, gently vortexed and then separated using a magnetic separator.
The beads were washed 4x with DT300 buffer, and labeled proteins were eluted in SDS-PAGE sample buffer, boiled 5 min, and then separated by SDS-PAGE on 8% gels.
Whole cell lysate was mixed with NuPAGE sample loading buffer (Invitrogen) containing DTT and then separated on a 4 10% SDS-PAGE gel and transferred to a polyvinylidene difluoride membrane.
HIV virions were exposed to buffer, CLR01 or CLR03 and then separated by centrifugation into a soluble fraction (containing free p24) and a sedimentable fraction (containing intact viral particles).
Pancreatic juice sample recovered from patients with pancreatic cancer and/or pancreatitis/benign tumor (control), containing 100 µg of total protein, were mixed with sample buffer, boiled for 5 min and then separated on 8 16% acrylamide gradient gels (Life-Gels).
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