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Overview
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Mass Spectrometry-grade rTrypsin-N Protease specifically hydrolyzes peptide bonds at the N-terminus of lysine (K) and arginine (R) residues. It is a mirror-image protease of trypsin and belongs to the family of N-terminal–cleaving proteases.
Physical Form: Mass spectrometry-grade rTrypsin-N protease is provided as a lyophilized powder.
Reconstitution: Dissolve in 40 µL of ultrapure water (pH 7.5) before use.
Shelf Life: 24 months when stored at –80°C.
pH Range: rTrypsin-N exhibits optimal activity at pH 7.5.
Application: rTrypsin-N specifically hydrolyzes peptide bonds at lysine (K) and arginine (R) sites of denatured proteins.
General Solution Digestion Method:
Recommended digestion buffer: 20–50 mM HEPES or Tris buffer.
Digestion conditions: Use the enzyme at a protein-to-enzyme ratio of 20:1 (w/w). Incubate at 37°C for more than 4 hours.
Cleavage Sites: R, KPlease contact us at for specific academic pricing.
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- Properties
- Applications
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Overview