Trypsin specifically cleaves peptide bonds at the C - terminus of lysine (K) and arginine (R). Due to the appropriate size of the generated peptide fragments, which are easy to be positively ionized, trypsin is the most commonly used tool protease in protein mass spectrometry characterization and proteomics research; it is also widely used in the production of peptide drugs. Aladdin's mass spectrometry - grade trypsin is recombinantly expressed in Pichia pastoris and purified by high - performance chromatographic methods. Meanwhile, trypsin is modified by methylation to avoid self - hydrolysis and digestion of trypsin, and to remove the activity of pseudochymotrypsin generated by self - cleavage.
Product Component Table
| R1374101 | Component | 100μg
| Storage |
| R1374101A | Trypsin | 100μg | -20℃. Avoid freeze/thaw cycle. |
| R1374101B | 1mM HCl | 300μl | -20℃. Avoid freeze/thaw cycle. |
Main Product Information
| Product Information | Details |
|---|
| Product Form | Protein Lyophilized Powder |
| Protein Molecular Weight | 23 kDa |
| Storage | Store the powder sample at -20°C |
| Dissolution Solution | 1 mM HCl or 50 mM Acetic Acid |
| Enzymatic Digestion Buffer | 50 mM Ammonium Bicarbonate or 50 mM Tris-HCl Solution with pH = 8.5 |
| Shelf Life | At -20°C, 2 years |
| Activity | ≥13000 U/mg protein |
| Definition of Enzyme Activity Unit | The difference in absorbance value per 0.001 at a wavelength of 253 nm per minute when trypsin reacts with substrate BAEE |
| pH Value | Applicable range: pH 8 - 9; pH < 3 will cause irreversible inactivation |
| Stability | Maximum concentrations tolerated by some reagents: 1% SDC, 0.1% SDS, 2 M Urea, 20% Acetonitrile |
| Enzymatic Digestion Site | Specifically hydrolyzes the peptide bond at the C - terminus of K and R amino acids in proteins |
Tips: For long - term storage, it is recommended to aliquot the dissolved enzyme and store it in a -20℃ refrigerator to avoid repeated freezing and thawing; for short - term storage: it can be stored at 4℃ for 7 days without significant loss of activity.
Usage Method:
1. Dissolve the trypsin lyophilized powder with 1mM HCl solution. For example: add 100μl of 1mM HCl to 100μg of trypsin to dissolve, prepare a 1μg/μl trypsin solution, aliquot into 10 tubes, and store 10μl in each tube.
2. The working solution of trypsin is 50mM ammonium bicarbonate, and the usage ratio of trypsin to the target protein is 1:50, that is, 1μg of trypsin can digest 50μg of protein solution sample.
3. After enzymatic cleavage at 37℃ overnight (16h), add formic acid to a concentration of 0.1% FA to terminate the enzymatic cleavage, and then perform subsequent mass spectrometry analysis.
Note: This product is for research use only and not for clinical purposes.
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