Catalase from bovine liver(2000-5000u/mg)
(Synonyms: 过氧化氢酶) 目录号 : GC64933Catalase是重要的抗氧化酶,在清除ROS。在维持氧化还原状态的平衡方面发挥着重要作用。Catalase与肿瘤的发生,发展关系密切。有潜力用于肿瘤的预防研究。
Cas No.:9001-05-2
Sample solution is provided at 25 µL, 10mM.
Quality Control & SDS
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- Biological Activity: 2000-5000u/mg
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
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].
References:
[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.
Cas No. | 9001-05-2 | SDF | |
别名 | 过氧化氢酶 | ||
Canonical SMILES | [Catalase] | ||
分子式 | 分子量 | ||
溶解度 | Water: 20 mg/mL ; DMSO: < 1 mg/mL (insoluble or slightly soluble) | 储存条件 | Store at -20°C |
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第一步:请输入基本实验信息(考虑到实验过程中的损耗,建议多配一只动物的药量) | ||||||||||
给药剂量 | mg/kg | 动物平均体重 | g | 每只动物给药体积 | ul | 动物数量 | 只 | |||
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% DMSO % % Tween 80 % saline | ||||||||||
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1. 首先保证母液是澄清的;
2.
一定要按照顺序依次将溶剂加入,进行下一步操作之前必须保证上一步操作得到的是澄清的溶液,可采用涡旋、超声或水浴加热等物理方法助溶。
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Interaction between pyridine adenine dinucleotides and bovine liver catalase: a chromatographic and spectral study
Arch Biochem Biophys 1986 Jul;248(1):71-9.PMID:3015030DOI:10.1016/0003-9861(86)90402-9.
Two different fractions were present in crystalline bovine liver catalase, and could be resolved using dye-ligand affinity chromatography with Red-A Matrex gel containing Procion HE 3B. The major part (alpha) was not adsorbed on this gel. The second fraction (beta) was firmly adsorbed to the gel, and could be eluted either by high salt or by NADPH in the micromolar range. Elution of catalase beta was also obtained with NADH, NADP+, and ADP at higher concentration. Fractions alpha and beta displayed no detectable difference in specific activity, stability to heat, and light absorption data. It is suggested that the difference in behavior between alpha and beta is related to the binding of NADPH to the mammalian catalase [H. N. Kirkman and G. F. Gaetani (1984) Proc. Natl. Acad. Sci. USA 81, 4343-4347], and that the beta fraction corresponds to the enzyme molecules that have at least one free site for NADPH binding. Modifications of catalase molecules in the presence of dithioerythritol (DTE) were examined using light absorption and EPR data. Thiol induced changes that corresponded to the formation of catalase complex II. They were partially reversed by NADPH at very low level, and the dinucleotide appeared to be oxidized in this process. DTE-treated bovine catalase was totally adsorbed on the Red-A Matrex columns, and could be eluted as fraction beta. Similar spectral changes in the presence of DTE and NADPH were displayed by a bacterial catalase from Proteus mirabilis. This enzyme was also able to oxidize NADPH, but was not adsorbed by Red-A Matrex. This work suggests that dye-affinity chromatography provides a very convenient tool for isolating dinucleotide-depleted Catalase from bovine liver, facilitating further study of the physiological function of this cofactor within the enzyme.