Protein fragmentation for sequencing: Endoproteinase Asp-N
Endoproteinase Asp-N is a metalloprotease that hydrolyzes peptide bonds on the amino terminus of aspartic and cysteic acid (oxidized cysteine). If the cysteine residue is reduced or alkylated, Endoproteinase Asp-N will cleave only the amino terminus of aspartic acid residues. The enzyme is supplied with a 250 mM sodium phosphate buffer (pH 8.0).
- Fragmentation of proteins and peptides required for primary structure analysis
Pseudomonas fragi mutant
Homogeneous on SDS-PAGE. No other proteases detected.
- Molecular weight: 27 kDa (SDS-PAGE)
- Optimum temperature: 37°C
- Optimum pH: 6.0–8.5
- Inhibitors: 2-phenanthroline, EDTA, DTT
Definition of activity
One azocoll unit is defined as the enzyme activity required to liberate azo dye to an absorbance of 0.001 at 520 nm per minute at 37°C at pH 7.5.
Specific Activity: 20 U/µg or more
Lyophilized (containing the equivalent of 50 µl of 10 mM Tris-HCl, pH 7.5)
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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