Protein analysis: Asparaginylendopeptidase
Asparaginylendopeptidase specifically cleaves peptide bonds on the carboxyl side of asparagine residues, including –Asn-Pro– bonds. The cleavage specificity of this enzyme has been validated on many peptides and proteins, confirming that bonds located on N-terminal or N-second position asparagine residues are not cleaved. Only those bonds adjacent to C-terminal asparagines residues are cleaved. Because asparagine residues bound to sugar chains are not cleaved, this enzyme can be used for protein analysis of sequenced glycoproteins. Asparaginylendopeptidase is isolated from Jackbean (Canavalia ensiformis).
- Peptide-bond cleavage
- Protein/peptide fragmentation prior to structural analysis
|Component||250 mM sodium acetate (pH 5.0), 50 mM DT, 5 mM EDTA|
Jackbean (Canavalia ensiformis)
No other proteases detected.
Protein samples must be denatured by chemical methods such as carboxymethylation prior to digestion with this enzyme.
|Molecular weight||37.000 kDa (SDS-PAGE)|
|Stable pH range||4.5–6.5|
|Thermal stability||Stable below 50°C|
|Inhibitors||p-chloromercuribenzoate (PCMB); N-ethylmaleimide (NEM)|
|Tolerance to denaturants|
|Less than or equal to 2 M urea|
|Less than or equal to 0.5 M guanidine-HCl|
|Less than or equal to 0.5% SDS|
In a solution of 20 mM sodium acetate buffer (pH 5.0) containing 50% glycerol, 0.005% Brij-35, 1 mM DTT, and 1 mM EDTA
0.2 mU/vial (5–10 uses for digestion of 2 nmol protein)
Definition of activity
One unit of activity corresponds to the amount of enzyme required to produce 1 µmol of DNP-Pro-Glu-Ala from DNP-Pro-Glu-Ala-Asn-NH2 in 1 minute at 37°C (pH 5.0).
Additional product information
Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.
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