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Products >  Protein_Research >  Protein_Sequencing_and_Analysis >  Protein_Fragmentation >  Arginylendopeptidase

Arginylendopeptidase

Arginylendopeptidase cleaves peptide bonds at the carboxyl side of arginine residues of proteins and peptides. Arginylendopeptidase is also known as mouse submaxillary protease D or as mouse EGF-binding protein C. This enzyme has been treated with TLCK and TPCK to remove trace trypsin-like and chymotrypsin-like protease activities. The product is supplied with 5X Reaction Buffer [250 mM sodium phosphate buffer (pH 8.0)].

Note: The enzyme has a weak activity toward -Lys-X- sites, especially when preceded by a basic amino acid residue.

At-A-Glance Documents

Applications

  • Fragmentation of proteins and peptides prior to structural analysis

Source

Mouse submaxillary glands

Purity

Homogeneous on SDS-PAGE. No other proteases detected.

Storage

–20°C

Properties

Molecular weight:21.3 kDa (gel filtration)
Optimum pH:8.0–9.0
Isoelectric point:5.65
Inhibitors: PMSF, DFP
Tolerance to denaturants:Less than or equal to 2 M Urea
Less than or equal to 0.1 M Guanidine-HCl
Less than or equal to 0.05% SDS

Form

Solution in 5 mM sodium phosphate buffer (pH 7.2) containing 50% glycerol

References

  1. Isackson, P. J. et al.. (1987) Biochemistry 26:2082.
  2. Matsushita, H. et al. (1988) Frontier Forum on Protein Microsequencing.
  3. Matsushita, H. et al. (1989) Protein, Nucleic Acid and Enzyme 34:374. (Japanese Journal)

Definition of Activity

One unit of enzyme activity corresponds to the amount required to produce 1 mmol p-nitroaniline from benzoyl-DL-arginine p-nitroanilide (BAPA) in 1 minute at 37°C, pH 8.0.




 
 
Products
Cat. # Product Package Size Price # of Units Select
7308 Arginylendopeptidase 0.5 mg $132.00
 

 



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