Trypsin Sequencing Grade, modified
ROCHE/TRYPSEQM-RO - from bovine pancreas
Synonym: Trypsin
Product Type: Chemical
| application(s) | life science and biopharma |
| biological source | bovine pancreas |
| color | white |
| concentration | 0.01-0.2 % (w/w) |
| foreign activity | Chymotrypsin |
| form | lyophilized (salt-free) |
| impurities | Chymotrypsin |
| manufacturer/tradename | Roche |
| mol wt | 24.000 g/mol |
| optimum pH | 8.0 |
| packaging | pkg of 4 × 100 μg (11418033001) |
| pkg of 4 × 25 μg (11418025001) | |
| Quality Level | 100  |
| solubility | 10 g/L |
| storage condition | ( |
| storage temp. | 2-8°C |
| suitability | suitable for protein modification |
| technique(s) | protein sequencing: suitable |
| UniProt accession no. |  |
| Analysis Note: | Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC. |
| Application: | Use Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins. It is used for:• Protein-structure elucidation • Tryptic mapping • Fingerprinting analysis • Sequence analysis • Translocation studies • Protein identification • Protein digestion during lipoprotein preparation for liquid chromatography-tandem mass spectrometry (LC-MS/MS) |
| Biochem/physiol Actions: | 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 Box) as a substrate. High concentrations of Trypsin Sequencing Grade, modified, one part by weight enzyme with 9 parts by weight insulin Box, are incubated for 18 hours to detect traces ofchymotrypsin impurities. |
| General description: | Trypsin Sequencing Grade, modified, is isolated from bovine pancreas as a highly purified and specific protease, and subsequently modified. Trypsin is a highly efficient and specific protease widely used in proteomics for protein digestion. It produces short peptides with specific characteristics that are compatible with current separation and identification methods such as liquid chromatography, mass spectrometry (MS). Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin,α1-antit |
| 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 weight Storage conditions (working solution): -15 to -25 °C Trypsin 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. |
| Preparation Note: | Store dry |
| Symbol |   GHS07,GHS08 |
| Signal word | Danger |
| Hazard statements | H315 - H319 - H334 - H335 |
| Precautionary statements | P261 - P264 - P280 - P284 - P304 + P340 + P312 - P342 + P311 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 3.4.21.4 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |