Catalase is a key enzyme in the metabolism of H₂O₂ and reactive oxygen species (ROS), and its expression and localization is markedly altered in tumors^[1]. Free oxygen radical scavenger.

Catalase, the enzyme that metabolizes H₂O₂ but also reacts with a multitude of other substrates. The active site of catalase contains an iron atom. Human catalase contains four identical subunits, each subunit containing four distinct domains and one prosthetic heme group. The four domains include: (1) a N-terminal arm which contains a distal histidine, an essential amino acid for the catalase reaction; (2) a β-barrel domain that contains eight β-barrels arranged in an antiparallel fashion with six α-helical insertions, conferring the hydrophobic core of the protein necessary for the tri-dimensional structure of the enzyme; (3) a connection domain which contains the tyrosine residue that binds the heme group; and finally (4) an α-helical domains, which is important for NADPH binding^[1].

上海金畔生物科技有限公司 has not independently confirmed the accuracy of these methods. They are for reference only.

9001-05-2

过氧化氢酶

Room temperature in continental US; may vary elsewhere.

H₂O : 33.33 mg/mL (Need ultrasonic)

DMSO : < 1 mg/mL (insoluble or slightly soluble)

• [1]. Glorieux C, et al. Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol Chem. 2017 Sep 26;398(10):1095-1108.