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[1] such as liquid chromatography, mass spectrometry (MS).[2]

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[3][4][5][6]
• 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