Endoproteinase Asp-N

Additional information

Brand

Size

2 ug

Endoproteinase Asp-N is a metalloprotease which specifically cleaves the peptide bonds at the amino side of aspartic acid or cysteic acid residues of proteins and peptides.

Applications

  • Fragmentation of proteins and peptides required for primary structure analysis

Source

Pseudomonas fragi mutant

Purity

Homogeneous on SDS-PAGE. No other proteases detected.

Properties

  • 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

Form

Lyophilized (containing the equivalent of 50 µl of 10 mM Tris-HCl, pH 7.5)

Effect of various denaturing agents on enzymatic activityEndoproteinase Asp-N (200 µg/mL) was treated with each denaturant at the indicated concentrationin 25 mM sodium phosphate buffer (pH 7

Effect of various denaturing agents on enzymatic activityEndoproteinase Asp-N (200 µg/mL) was treated with each denaturant at the indicated concentrationin 25 mM sodium phosphate buffer (pH 7

Effect of various denaturing agents on enzymatic activity

Endoproteinase Asp-N (200 µg/mL) was treated with each denaturant at the indicated concentrationin 25 mM sodium phosphate buffer (pH 7.8). The enzyme was exposed to denaturant for 6 hours at 25°C, then enzyme activity was measured.