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Equimolar amounts of the BACs were mixed and digested with PvuII, which was followed by ligation in 20 μl.
Equal amounts of protein (2.5 mg) extracted from each cell population were mixed and digested with trypsin.
Proteins were extracted from a SILAC (stable isotope labeling by amino acids in cell culture) labeled and an unlabeled strain, mixed and digested enzymatically.
Eighteen purified recombinant proteins were mixed and digested by trypsin into peptide mixtures, which were then analyzed by LC-MS/MS on diverse mass spectrometers under various conditions.
Proteins, extracted from a SILAC (stable isotope labeling by amino acids in cell culture) labeled and an unlabeled yeast strain were mixed and digested enzymatically in solution.
The light (normal) and heavy (cancer) N-terminus/lysine labeled serum glycopeptides were mixed and digested with PNGase F to cleave the N-glycans from peptides according to the protocol described elsewhere [ 51].
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Specimens were minced and digested enzymatically (Dispase I, overnight).
The saturated α-cyano-4-hydroxycinnamic matrix was prepared in acetonitrile/aqueous TFA 0.4% (3∶2), mixed with digested samples and applied to a stainless-steel probe plate.
Purified partial digests were mixed with digested, phosphatased vector DNA in titration experiments and scored by transformation in E coli, solely as a means of determining the number of successful ligations.
Equimolar amounts of amplicons were mixed, BamHI digested, re-ligated, purified by ethanol precipitation and dissolved in H2O.
Equal amounts of mono-nucleosomal DNA and digested genomic DNA (2 μg) were labeled with Cy5 and Cy3 respectively, mixed and hybridized to array using manufacturer's protocol.
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