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Products >  Protein_Research >  Protein_Sequencing_and_Analysis >  Protein_Fragmentation >  Endoproteinase_Asp-N

Endoproteinase Asp-N

Endoproteinase Asp-N is a metalloprotease that hydrolyzes peptide bonds on the amino side of Asp and Cys oxidized to cysteic acid. If cysteine is reduced or alkylated, the enzyme will cleave only the amino side of Asp residues. The enzyme is supplied with 250 mM sodium phosphate buffer (pH 8.0).

At-A-Glance Documents

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 $144.00
 

 



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