Asparaginylendopeptidase
Applications:
- Fragmentation of Proteins and Peptides Prior to Structural Analysis
Description:
Asparaginylendopeptidase specifically cleaves peptide bonds on the carboxyl side of asparagine residues, including –Asn-Pro– bonds. The substrate specificity of this enzyme has been validated on many peptides and proteins. The bonds next to N-terminal or N-second position asparagine residues will not be cleaved with this enzyme. Bonds adjacent ot C-terminal asparagines residues are cleaved. Also, because asparagine residues bound to sugar chains are not cleaved, this enzyme can be used to estimate the attachment sites of sugars in glycoproteins of known sequence. Asparaginylendopeptidase is isolated from Jack bean.
Purity:
No other proteases detected.
Form:
Solution in 20 mM sodium acetate buffer (pH 5.0) containing 50% glycerol, 0.005% Brij-35, 1 mM DTT and 1 mM EDTA
Volume: 0.2 mU/vial (5–10 uses for digestion of 2 nmol protein)
Definition of Activity:
One unit of enzyme activity corresponds to the amount required to produce 1 µmol of DNP-Pro-Glu-Ala from DNP-Pro-Glu-Ala-Asn-NH2 in 1 minutes at 37°C, pH 5.0.
Source:
Jack bean
Properties:
| Molecular weight: | 37,000 (SDS-PAGE) |
| Optimum pH: | 5.5–6.5 |
| Stable pH range: | 4.5–6.5 |
| Optimum temperature: | 37–45°C |
| Thermal stability: | Stable below 50°C |
| Inhibitors: | p-chloromercuribenzoate (PCMB); N-ethylmaleimide (NEM) |
| Tolerance to denaturants: | |
| Stable against | ≤ 2 M urea |
| ≤ 0.5 M guanidine-HCl | |
| ≤ 0.5% SDS | |
Supplied Buffer (5X)
| Volume: | 1 mL |
| Component: | 250 mM Sodium acetate, pH 5.0, 50 mM DT, 5 mM EDTA |
Storage:
–20°C
Notes:
It is necessary to denature the protein samples by chemical procedure such as carboxymethylation, prior to digestion with this enzyme.
Limited Use Label License: [M32]
