Not available outside of the UK & Ireland.

Application

Use Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins.It is used for:Protein-structure elucidationTryptic mappingFingerprinting analysisSequence analysisTranslocation studiesProtein identification

General description

Trypsin Sequencing Grade, modified, is isolated from bovine pancreas as a highly purified and specific protease, and subsequently modified.Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, A2-macroglobulin,A1-antitrypsin, APMSF, and antipain.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Preparation Note

Working concentration: 1/100 to 1/5 of the protein by weightStorage conditions (working solution): -15 to -25 °CTrypsin Sequencing Grade, modified, is more resistant to autolysis, even at pH values in the neutral and weakly basic range. The enzyme can be used in high concentrations.A solution in 1% acetic acid or 1 mM HCI can be used for up to one week when stored at 2 to 8° C. Stored in aliquots at -15 to -25 °C, the solution is stable for at least one year without loss of activity.

Quality

Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.

Specificity

Trypsin is a serine endopeptidase. At pH 7.5–9, it specifically hydrolyzes proteins and peptide bonds C-terminally of Iysine and arginine. Amide and ester bonds of Arg and Lys are also cleaved. The specificity of Trypsin Sequencing Grade, modified, is verified with the oxidized B-chain of insulin (insulin B_ox) as a substrate. High concentrations of Trypsin Sequencing Grade, modified, one part by weight enzyme with 9 parts by weight insulin B_ox, are incubated for 18 hours to detect traces ofchymotrypsin impurities.