'Gold standard' for MS grade trypsin

Promega's new Trypsin Gold, mass spectrometry grade,provides researchers with a protease that far exceeds nativetrypsin in terms of specificity, purity and robustness.Especially produced for mass spectrometry (MS) proteomicresearch, peptide fragments generated by Trypsin Gold aresuitable for reliable and accurate mass spectrometric databaseanalysis.

Building on the quality reputation of Promega'ssequencing grade trypsin, Trypsin Gold has been manufactured tostringent quality standards to guarantee specificity.

Beforedispatch, each lot of Trypsin Gold is quality tested using MS toensure its reliability and reproducibility in generating peptidesfrom in-gel digests.

The specificity of this highly purifiedtrypsin is enhanced by treatment with TPCK, which inactivateschymotrypsin.

Lysine residues in the enzyme have been methylated,yielding a highly active and stable molecule that is extremelyresistant to autolytic digestion.

Trypsin Gold is also resistantto mild denaturing conditions such as 0.1% SDS and retains 50%activity in 2M guanidineHCl.

The enzyme is provided in a singlevial and its stability is ensured for up to five freeze/thawcycles, minimising waste.

Mass spectrometry requires highlypurified proteases exhibiting maximum specificity.

It isessential that any enzymes used to cleave proteins for subsequentMS analysis do so in a reproducible manner in order for theproteins to be accurately identified.

Trypsin Gold greatlyexceeds native trypsin in quality and performance as nativetrypsin is subject to autolysis, generating pseudotrypsin, whichexhibits broadened specificity.

This can result in the presenceof additional peptide fragments that can interfere with databaseanalysis of MS results.