The default search settings used for protein identification were trypsin cleavage with fixed iodoacetamide modification of cysteine.
The default search settings used for quantitative analysis and protein identification were: trypsin cleavage with fixed MMTS modification of cysteine, iTRAQ labeling and variable methionine oxidation.
The default search settings used for quantitative analysis and protein identification were: trypsin cleavage with fixed MMTS modification of cysteine, iTRAQ labelling and variable methionine oxidation.
The sepharose was washed four times and UBXN7 was recovered upon cleavage with TEV protease.
The His-tag was removed by cleavage with AcTEV protease (Invitrogen), and the proteins were further purified by anion-exchange.
Tryptase was active following cleavage with a SUMOstar specific protease.
Tag-free protein was generated by cleavage with PreScission protease.
The untagged protein was obtained after cleavage with TEV-protease followed by two passages over Nickel-Sepharose.
The Sumo-6His tag was removed by cleavage with Ulp1 (Sumo Protease) followed by Ni-NTA subtraction.
Spätzle itself is synthesised as an inactive proprotein and is activated by cleavage with serine proteases [ 46] including trypsin [ 44].
