TRYPSEQM-RO

Trypsin Sequencing Grade, modified

from bovine pancreas

• Synonym(s): Trypsin
• UNSPSC Code: 12352204
• EC Number: 3.4.21.4 (BRENDA, IUBMB)
• NACRES: NA.54
• Biological source: bovine pancreas
• Concentration: 0.01-0.2 % (w/w)

Properties

• biological source: bovine pancreas
• form: lyophilized (salt-free)
• mol wt: 24.000 g/mol
• packaging: pkg of 4 × 100 μg (11418033001), pkg of 4 × 25 μg (11418025001)
• manufacturer/tradename: Roche
• storage condition: (Keep container tightly closed in a dry and well-ventilated place.)
• concentration: 0.01-0.2 % (w/w)
• technique(s): protein sequencing: suitable
• impurities: Chymotrypsin
• color: white
• optimum pH: 8.0
• solubility: 10 g/L
• suitability: suitable for protein modification
• UniProt accession no.: P00760
• application(s): life science and biopharma
• foreign activity: Contaminating activities corresponds; Chymotrypsin , contains
• storage temp.: 2-8°C
• Gene Information: cow ... PRSS1(780933)

Description

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-antitrypsin, APMSF, and antipain.

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 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.

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.

Store dry

Analysis Note

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

Other Notes

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

Safety Information

• pictograms: GHS07,GHS08
• signalword: Danger
• pcodes: P261 - P264 - P280 - P284 - P304 + P340 + P312 - P342 + P311
• Hazard Classifications: Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
• target_organs: Respiratory system
• Storage Class: 11 - Combustible Solids
• wgk: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• hcodes: H315,H319,H334,H335