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C3556

Sigma-Aldrich

Catalase from human erythrocytes

≥90% (SDS-PAGE), buffered aqueous solution, ≥30,000 units/mg protein

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Synonym(s):
H2O2:H2O2 oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

human erythrocytes

Quality Level

assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

specific activity

≥30,000 units/mg protein

mol wt

tetramer ~250 kDa

storage condition

(Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons)

concentration

≤10 mg/mL

technique(s)

cell based assay: suitable

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

InChI

1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3

InChI key

NUVBSKCKDOMJSU-UHFFFAOYSA-N

Gene Information

human ... CAT(847)

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C3155E3289C1345
Sigma-Aldrich

C3556

Catalase from human erythrocytes

Sigma-Aldrich

C3155

Catalase from bovine liver

Catalase from bovine liver ≥20000 units/mg protein, lyophilized powder

E3289

Catalase from bovine liver

Catalase from bovine liver powder, suitable for cell culture, 2,000-5,000 units/mg protein

C1345

Catalase from bovine liver

assay

≥90% (SDS-PAGE)

assay

-

assay

-

assay

-

Gene Information

human ... CAT(847)

Gene Information

cow ... CAT(280743)

Gene Information

-

Gene Information

cow ... CAT(280743)

specific activity

≥30,000 units/mg protein

specific activity

≥30,000 units/mg protein

specific activity

≥20000 units/mg protein

specific activity

2,000-5,000 units/mg protein

technique(s)

cell based assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

cell culture | mammalian: suitable

form

buffered aqueous solution

form

aqueous solution

form

lyophilized powder

form

powder

General description

Research area: Cell Signaling

Human catalase is a member of the monofunctional heme-containing catalases. It is an intracellular enzyme located at higher concentrations in the liver, erythrocytes, and kidney. Catalase is a homo-tetrameric protein and comprises amino acid residues, one heme group that is iron III protoporphyrin IX, and a nicotinamide adenine dinucleotide phosphate (NADPH) molecule. It is a ubiquitous enzyme found in most aerobic organisms. The catalase (CAT) gene is located on the human chromosome at 11p13.

Application

Catalase from human erythrocytes has been used:

  • to prevent reoxidation of reduced cytochrome c by H2O2 while measuring the production of superoxide with cytochrome C.
  • as a component of the imaging buffer for stochastic optical reconstruction microscopy (STORM) imaging of human skin fibroblasts
  • as a component of the gloxy mix for single-molecule imaging

Biochem/physiol Actions

Deficiency of catalase and oxidative stress are associated with vitiligo, hypertension, Alzheimer′s disease, diabetes mellitus, and acatalasemia. Catalase shows a dichotomous role in cancer as its expression is at a higher level in chronic lymphocytic leukemia, glioma, melanoma, and gastric cancer and lower levels of expression are seen in acute myeloid leukemia, pancreatic, lung, prostate, and skin (non-melanoma) cancers.
Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis.

Unit Definition

One unit will decompose 1.0 μmole of H2O2 per min at pH 7.0 at 25 °C, while the H2O2 conc. falls from 10.3 to 9.2 mM, measured by the rate of decrease of A240.

Physical form

Solution in 50 mM Tris, pH 8.0

Analysis Note

Protein determined by biuret

inhibitor

Product No.
Description
Pricing

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Urte Neniskyte et al.
Methods in molecular biology (Clifton, N.J.), 1041, 103-111 (2013-07-03)
Reactive oxygen and nitrogen species are both regulators and effectors of microglial activation, and assays of these oxidants can be used as a measure of acute and chronic activation of microglial cells. Here we describe quick methods to assess the
Investigation of the binding mechanism and inhibition of bovine liver catalase by quercetin: Multi-spectroscopic and computational study
Samaneh R, et al.
BioImpacts, 7(3), 147?153-147?153 (2017)
D A Chistiakov et al.
Diabetes/metabolism research and reviews, 20(3), 219-224 (2004-05-11)
Oxidative stress is involved in the origin of type 1 diabetes. Low efficiency of the scavenging antioxidant system has been shown to be related to the pathogenesis of the disease. This, therefore suggests that genes encoding catalase and other antioxidant
Li-Wen Shen et al.
Acta pharmacologica Sinica, 43(1), 177-193 (2021-07-24)
Inhibition of autophagy has been accepted as a promising therapeutic strategy in cancer, but its clinical application is hindered by lack of effective and specific autophagy inhibitors. We previously identified cepharanthine (CEP) as a novel autophagy inhibitor, which inhibited autophagy/mitophagy
J Kodydková et al.
Folia biologica, 60(4), 153-167 (2014-08-26)
Catalase (CAT) is a well-studied enzyme that plays an important role in protecting cells against the toxic effects of hydrogen peroxide. In human, it has been implicated in different physiological and pathological conditions. This review summarizes the information available on

Articles

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

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