Protease (S. Aureus) V.8

Protease V.8 specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. In the presence of ammonium, the specificity is limited to glutamic sites.


This lyophilized enzyme is from Bacillus thermoproteolyticus. This enzyme is characterized by its excellent heat stability and substrate specificity towards isoleucine, methionine and valine. Activity: 7000 PU/mg of protein.


Tryptase (Purified Antigen)

Tryptase is a glycoprotein released from mast cells during anaphylaxis, which performs a number of functions including catalyzing the activation of complement C3, converting prostromelysin to stromelysin (MMP-3), and cleaving fibrinogen resulting in a loss of clotting potential. Human tryptase is a major secretory protease of human lung mast cells.


(1,4-β-Xylan xylohydrolase, EC
From Trichoderma viride
Activity: 5 U/vial
Unit Definition: One unit is defined as the amount of enzyme required to liberate 1 μmole of p-nitrophenol from p-nitrophenyl-α-D-xylopyranoside per minute at 37°C, pH 4.0.

Horseradish Peroxidase (Rz >3.0)

Horseradish peroxidase (HRP) is isolated from horseradish roots and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme.