C3556
Catalase from human erythrocytes
≥90% (SDS-PAGE), buffered aqueous solution, ≥30,000 units/mg protein
Synonym(s):
H2O2:H2O2 oxidoreductase
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
| Pack Size | SKU | Availability | Price |
|---|
About This Item
CAS Number:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
232-577-1
MDL number:
eCl@ss:
32160410
Specific activity:
≥30,000 units/mg protein
Assay:
≥90% (SDS-PAGE)
Biological source:
human erythrocytes
Concentration:
≤10 mg/mL
Pricing and availability is not currently available.
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
concentration
≤10 mg/mL
technique(s)
cell based assay: suitable
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
SMILES string
O(CC)C(=O)c1ccc(cc1)O
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)
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.[1] It is a ubiquitous enzyme found in most aerobic organisms.[2] The catalase (CAT) gene is located on the human chromosome at 11p13.[3]
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.[1] It is a ubiquitous enzyme found in most aerobic organisms.[2] The catalase (CAT) gene is located on the human chromosome at 11p13.[3]
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.[4]
- as a component of the imaging buffer for stochastic optical reconstruction microscopy (STORM) imaging of human skin fibroblasts[5]
- as a component of the gloxy mix for single-molecule imaging[6]
Biochem/physiol Actions
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.
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.[2]
Physical form
Solution in 50 mM Tris, pH 8.0
Preparation Note
Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons
persons
Analysis Note
Protein determined by biuret
Other Notes
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.
1 of 1
This Item | |||
|---|---|---|---|
| Gene Information human ... CAT(847) | Gene Information - | Gene Information - | Gene Information - |
| biological source human erythrocytes | biological source bacterial (Corynebacterium glutamicum) | biological source bacterial (Micrococcus lysodeikticus) | biological source - |
| technique(s) cell based assay: suitable | technique(s) - | technique(s) microbe id | metabolite detection: suitable | technique(s) - |
| assay ≥90% (SDS-PAGE) | assay - | assay - | assay - |
| specific activity ≥30,000 units/mg protein | specific activity - | specific activity 65,000-150,000 U/mL | specific activity ≥10,000 units/mg protein, ≥4000 units/mg dry wt. |
| concentration ≤10 mg/mL | concentration ≥500000 U/mL | concentration - | concentration - |
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C3556-.5MG | 04061833486016 |