Endoproteinase Asp-N, Sequencing Grade
from a mutant of Pseudomonas fragi, lyophilizate
For further processing only.
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Endoproteinase Asp-N, Sequencing Grade material number and pack size: Material Number Pack Size 11058541103 2 μg
Endoproteinase Asp-N can be used for specific cleavage of peptides.
Endoproteinase Asp-N is a widely used metalloprotease, that specifically hydrolyzes peptide bonds at the amino side of aspargine and cysteine.
If cysteine is reduced or alkylated only -↓-Asp-X is cleaved. Endoproteinase Asp-N is isolated from Pseudomonas fragi mutant. The protease is supplied as lyophilizate.
- Obtain consistent and clear peptide sequencing results.
- Minimize the risk of unknown peptide impurities by using this highly purified quality.
- Use Endoproteinase Asp-N, Sequencing Grade, for protein structure analysis and sequence analysis.
Molecular weight: 27 kD
pH optimum: 7.0-8.0
Inhibitors: EDTA and α-phenanthroline Appearance: White lyophilized substance
Activity (+37°C, with azocoll): ≥40 U/bottle
Specific activity: ≥20,000 U/mg protein
SDS PAGE (homogeneity; phastSystem®, 8-25%): ≥90%
Specificity (HPLC, with glucagon, cleavage after 1 h): ≥90%
Unspecific cleavage products (HPLC, melittin, after 4 hours incubation): ≤10%
Stability: At +2 to +8°C within specification range for 12 months; stored dry.