Especially produced for mass spectrometry (MS) proteomic research, peptide fragments generated by Trypsin Gold are suitable for reliable and accurate mass spectrometric database analysis
Promega's new Trypsin Gold, mass spectrometry grade, provides researchers with a protease that far exceeds native trypsin in terms of specificity, purity and robustness. Especially produced for mass spectrometry (MS) proteomic research, peptide fragments generated by Trypsin Gold are suitable for reliable and accurate mass spectrometric database analysis.
Building on the quality reputation of Promega's sequencing grade trypsin, Trypsin Gold has been manufactured to stringent quality standards to guarantee specificity.
Before dispatch, each lot of Trypsin Gold is quality tested using MS to ensure its reliability and reproducibility in generating peptides from in-gel digests.
The specificity of this highly purified trypsin is enhanced by treatment with TPCK, which inactivates chymotrypsin.
Lysine residues in the enzyme have been methylated, yielding a highly active and stable molecule that is extremely resistant to autolytic digestion.
Trypsin Gold is also resistant to mild denaturing conditions such as 0.1% SDS and retains 50% activity in 2M guanidineHCl.
The enzyme is provided in a single vial and its stability is ensured for up to five freeze/thaw cycles, minimising waste.
Mass spectrometry requires highly purified proteases exhibiting maximum specificity.
It is essential that any enzymes used to cleave proteins for subsequent MS analysis do so in a reproducible manner in order for the proteins to be accurately identified.
Trypsin Gold greatly exceeds native trypsin in quality and performance as native trypsin is subject to autolysis, generating pseudotrypsin, which exhibits broadened specificity.
This can result in the presence of additional peptide fragments that can interfere with database analysis of MS results.
