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Products >  Protein_Research >  Protein_Sequencing_and_Analysis >  Protein_Fragmentation >  Endoproteinase_Asp-N

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).

At-A-Glance Documents Images & Data Resources

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 unit of enzyme activity corresponds to the amount required to increase 0.001 absorbance unit of the peptide soluble in trichloro-acetic acid at 280 nm in 1 minute at 37°C, pH 8.0 using casein as the substrate.

Activity: Approximately 14 U/µg protein

Form

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




 
 
Products
Cat. # Product Package Size Price # of Units Select
7329 Endoproteinase Asp-N 2 ug $147.00
 

 


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