肽鏈內(nèi)切酶Lysyl Endopeptidase（R）

規(guī)格: 1 vial （2 AU） , 1 vial （10 AU）
Grade: for Biochemistry
Summary
 
This product is for research use only. Do not administer it to human.

Purity: Homogenous on SDS-PAGE

Activity: shown on each label. Unit: AU*/vial
* AU: Amidase Unit - amount of enzyme required for the formation of 1 umol of p-nitroaniline from
N-benzoyl-DL-lysine-p-nitroaniline per minute at 30 degrees C, pH 9.5.

Preparation A 10AU-vial contains Tris-HCl corresponding to 1 mL of 2 mM Tris HCl buffer （pH 8.0）.
Molecular Weight] 27,000 （gel filtration）; 30,000 （SDS electrophoresis）
Optimal pH 9.0 -9.5 （amidase activity）
Stability Very stable in lyophilized forms at -20 degrees C; Stable for at least 2 years at -20 degrees C
when dissolved in Tris-HCl buffer at pH 4.0 to 11 at the enzyme concentration of more than 1 mg/mL. Stable for at
least 24 hours at 4 degrees C under the above conditions.

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 degrees C.

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