Thermolysin, Geobacillus stearothermophilus

Native thermolysin from Geobacillus stearothermophilus. A highly thermostable zinc metallo-endoproteinase that exhibits specificity toward isoleucine, leucine, methionine, and valine. Inhibitors include EDTA, 1,10-phenathroline, phosphinates, and phosphoamidates. Not inhibited by aprotinin or other serine protease inhibitors. Contains a zinc atom essential for activity and four Ca²⁺ essential for thermal and conformational stability. Has an optimal pH in the range 7.0-9.0.

Native thermolysin from Geobacillus stearothermophilus. Zinc metalloendoproteinase with specificity toward isoleucine, leucine, methionine and valine. Inhibitors include EDTA, 1,10-phenanthroline, phosphinates, and phosphoamidates. Not inhibited by aprotinin or other serine protease inhibitors. Contains a zinc atom essential for activity and four Ca²⁺ essential for thermal and conformational stability. Note: 1 KU = 1000 units.

Note: 1 KU = 1000 units.

Please refer to vial label for lot-specific concentration.

Lyophilized solid containing calcium acetate, sodium acetate, 3X crystallized.

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.

Reconstitute in 42% glycerol adjusted to pH 8.0 with 0.01 N NaOH, containing 0.005% Triton^™ X-100 detergent.

One protease unit is defined as the amount of the enzyme that liberates the non-proteinous digestion product from milk casein at final concentration of 0.5% to give Folin′s color equivalent to 1 µg of tyrosine per min at the early stage of the reaction at 35°C, pH 7.2.

Pfuetzner, R.A. and Chan, W.W. 1993. Eur. J. Biochem. 218, 523.
Matsubara, H. 1970. Methods Enzymol. 19, 642.
Ohta, Y., et al. 1966. J. Biol. Chem.241, 5919.

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Toxicity: Harmful (C)