Protein digestion: arginylendopeptidase
Arginylendopeptidase cleaves peptide bonds at the carboxyl side of arginine residues located on proteins and peptides, enabling protein fragmentation for structural analysis. Arginylendopeptidase is also known as mouse submaxillary protease D or 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 a 5X Reaction Buffer [250 mM sodium phosphate buffer (pH 8.0)].
NOTE: This enzyme has weak activity towards -Lys-X- sites, especially when those sites are preceded by a basic amino acid residue.
- Protein digestion
- Fragmentation of proteins and peptides prior to structural analysis
Mouse submaxillary gland
|Molecular weight||21.3 kDa (gel filtration)|
|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
In a solution of 5 mM sodium phosphate buffer (pH 7.2) containing 50% glycerol.
Definition of activity
One unit of activity corresponds to the amount of enzyme required to produce 1 mmol p-nitroaniline from benzoyl-DL-arginine p-nitroanilide (BAPA) in 1 min at 37°C and pH 8.0.
Isackson PJ, Silverman RE, Blaber M, Server AC, Nichols RA, Shooter EM, Bradshaw, R. Epidermal growth factor binding protein: identification of a different protein. Biochemistry 26, 2082-5 (1987).
Matsushita H, Kato I, Aoyama H, Tsunasawa S, S. F. Arginylendopeptidase. Protein, Nucleic Acid Enzym. (Japanese Journal) 34, 374-9 (1989).
Schenkein, I., Levy, M., Franklin, E.C., Frangione, B. Proteolytic enzymes from the mouse submaxillary gland. Specificity restricted to arginine residues. Arch Biochem Biophys. 182, 64-70 (1977).
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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