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Briefly, pol V and RecA proteins at various known concentrations were resolved on an SDS-PAGE gel (10%) as standards and gel band intensities were quantified using IMAGEQUANT software.
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The purity and concentration was resolved and calculated by the A260/A280 ratio and A260 absorption value.
Equivalent concentration of proteins were resolved on 10% SDS-PAGE and transferred to polyvinylidene difluoride membranes.
HepG2 cells were treated with uttroside B for 48 h at different concentrations and the WCL were resolved on an 8% gel, immunoblotted against anti-PARP and detected by ECL.
Cell extracts were boiled for 5 min and equal concentrations of cell lysates were resolved on a SDS-NuPage gel.
After determining the protein concentration, twenty micrograms of proteins were resolved on Bis-Tris gels (Invitrogen) and transferred onto nylon membranes.
Equal amounts of p17 protein in solution under different NaCl concentrations (0.5, 0.2 and 0.1 M) were resolved on a 12% SDS-polyacrylamide gel and then electroblotted onto a nitrocellulose membrane.
Equal concentrations of protein extracts (100 μg) were resolved by sodium dodecyl sulfate-PAGE and transferred to a nitrocellulose membrane (Bio-Rad, Hercules, CA, USA).
Equal concentrations of protein samples (60 µg) were resolved by 4 20% gradient SDS PAGE (Pierce, Rockford, IL, USA) and transferred to nitrocellulose membranes (Millipore Corp., Billerica, MA, USA) for subsequent immunoblot experiments.
Bradford assay (Bio-Rad, Hercules, CA, USA) was used to determine protein concentration and 75 μg of proteins were resolved in 8.5 or 10% SDS-PAGE gels.
Equal concentrations (30 μg) of nuclear protein extracts were resolved by electrophoresis on 7.5% SDS-polyacrylamide gels.
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