rAsp-N Protease, 1800u, Mass Spectra Grade

Mass Spectrometry-grade Asp-N Protease is a metalloprotease that specifically cleaves peptide bonds at the N-terminus of aspartic acid (D) residues. It exhibits specific activity in phosphate, acetate, or Tris buffers within the pH range of 6.0–8.5.

Physical Form: Mass spectrometry-grade Asp-N protease is provided as a lyophilized powder (in 10 mM Tris-HCl).
Reconstitution: Dissolve in 50 µL of ultrapure water before use.
Shelf Life: 12 months when stored at –80°C.
pH Range: Asp-N exhibits optimal activity at pH 7–8.
Application: Asp-N protease specifically hydrolyzes peptide bonds at aspartic acid (D) residues of denatured proteins.

General Solution Digestion Method:
Use the enzyme at a 1:50 (w/w) enzyme-to-protein ratio and incubate in a 37°C water bath for 4 hours.

Recommended Buffer:
10 mM Tris-HCl buffer, pH 7.5. To prevent autolysis, the incubation temperature should not exceed 37°C.

Cleavage Sites: D

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