Lysyl Endopeptidase is a protease secreted by the soil bacterium Achromobacter lyticus M497-1, and is synonymous with the achromobacter protease discovered by Masaki, et al. Lysyl Endopeptidase cleaves peptide bonds at the carboxy-terminal of both lysine residues and S-aminoethylcysteine residues with a high degree of specificity, making it a valuable tool for analysis of peptide and protein primary structure and for enzymatic synthesis of Lys-X compounds. An added feature of Lysyl Endopeptidase is its ability to retain complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30°C.
Among the most important techniques in proteome analyses is the in-gel digestion of protein spots/bands that have been resolved by electrophoresis using digestive enzymes, such as trypsin and lysyl endopoptidase. Proteins can be identified by mass spectrometry analysis of the peptides produced by in-gel digestion, and further information regarding post-translational modifications can be obtained. Lysyl Endopeptidase, Mass Spectrometry Grade is a freeze dried product that has sufficient activity for in-gel digestion and packed in very small quantities for convenience purposes.
Unit Definition:1AU: Amidase Unit is the amount of enzyme required for the formation of 1umol of p-nitroaniline from N-benzoyl-DL-lysine-p-nitroaniline per minute at 30°C, pH 9.5.
Activity:0.03-0.07 AU/vial
Optimal pH:9.0-9.5 (amidase activity)
Applications:Suitable for use in Sequencing. Other applications not tested.
Isoelectric Point:6.9-7.0
Storage and Stability:Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with 2mmol/L Tris-HCl, pH 8.0. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：5x20ug
Source Antigen：Lysobacter
Form：Supplied as a powder lyophilized from a solution containing 2mmol/L Tris-HCl buffer, pH 8.0.
