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Merck

C3515

Sigma-Aldrich

Catalase from Aspergillus niger

ammonium sulfate suspension, ≥4,000 units/mg protein

Szinonimák:

H2O2:H2O2 oxidoreductase

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
MDL-szám:
UNSPSC kód:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biológiai forrás

Aspergillus niger

Minőségi szint

form

ammonium sulfate suspension

specifikus aktivitás

≥4,000 units/mg protein

molekulatömeg

tetramer ~250 kDa

tárolási körülmény

(Tightly closed)

technika/technikák

FISH: suitable

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

2-8°C

InChI

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

Nemzetközi kémiai azonosító kulcs

NUVBSKCKDOMJSU-UHFFFAOYSA-N

Általános leírás

Research area: Cell Signaling

Catalase is an active enzyme present in aerobic organisms. It is a ferric hemoprotein and a tetramer.

Alkalmazás

Catalase from Aspergillus niger has been used:
  • as a positive control during the functional characterization of Clostridium difficile spore coat proteins.
  • as a component of the catalase solution to prepare GLOX buffer with enzymes to maintain the embryos of Caenorhabditis elegans before single-molecule fluorescence in situ hybridization (smFISH) studies
  • as a component of the imaging buffer for stochastic optical reconstruction microscopy (STORM) imaging of platelet-rich plasma
  • as a supplement in Todd Hewitt media plus 0.5 % yeast extract (THY) media for the neutralization of pneumococcal H2O2

Biokémiai/fiziológiai hatások

Catalase catalyzes the decomposition of hydrogen peroxide into water and oxygen. Each subunit of the tetramer contains iron bound to a protoheme IX group. The enzyme also strongly binds NADP, which is in close proximity to the heme group. Isoelectric point is found to be 6.5. Optimum pH for catalytic activity is 7.0. The enzyme activity is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogen bromide, 2-mercaptoethanol, dithiothreitol, dianisidine, and nitrate. Incubation of catalase with ascorbate or ascorbate/Cu2+ results in degradation of the catalase molecule.
Catalase is involved in catalyzing the degradation of hydrogen peroxide (H2O2) to water and free oxygen. Catalase is used commercially for decomposing H2O2 as it is added as an antimicrobial agent in process streams. It also catalyzes the oxidation of electron donors like ethanol and phenols during lower concentrations of H2O2. Catalase shows antioxidant activity by protecting cells from higher levels of reactive oxygen species (ROS). Increased expression of catalase is observed in chronic lymphocytic leukemia, gastric cancer, glioma, and melanoma. Decreased levels of catalase are seen in acute myeloid leukemia, lung, pancreatic, prostate, and skin (non-melanoma) cancers. Hence catalase exhibits a dual role in cancer.

Vigyázat

Freezing of solutions is not recommended.

Egység definíció

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

Fizikai forma

Suspension in 3.2 M (NH4)2SO4 solution, pH 6.0

Analízis megjegyzés

Protein determined by biuret

Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

L Brunelli et al.
Free radical biology & medicine, 30(7), 709-714 (2001-03-29)
Previously, we found that catalase enhanced the protection afforded by superoxide dismutase to Escherichia coli against the simultaneous generation of superoxide and nitric oxide (Brunelli et al., Arch. Biochem. Biophys. 316:327-334, 1995). Hydrogen peroxide itself was not toxic in this
3D structure modeling of catalase enzyme from Aspergillus Fumigatus
Dwivedi V D, et al.
Open journal of immunology, 1(1) (2016)
J Fiedurek et al.
Journal of applied microbiology, 89(1), 85-89 (2000-08-17)
A novel method for increasing dissolved oxygen concentration in culture media has been developed. It involves adding hydrogen peroxide (H2O2) to the medium which is then decomposed to oxygen and water by catalase. Some factors affecting oxygenation of culture were
Seleipiri Charles et al.
Analytical chemistry, 93(3), 1369-1376 (2020-12-24)
Recent development in fluorescence-based molecular tools has contributed significantly to developmental studies, including embryogenesis. Many of these tools rely on multiple steps of sample manipulation, so obtaining large sample sizes presents a major challenge as it can be labor-intensive and
M E Percy
Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire, 62(10), 1006-1014 (1984-10-01)
Although animal catalase has been studied for decades, its physiological role has remained perplexing. It has two enzymatic functions, not only catalyzing the breakdown of H2O2 into O2 and H2O, but also in the presence of low concentrations of H2O2

Cikkek

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Az ammónium-szulfát szuszpenzióként szállított enzimekkel való munkavégzésre vonatkozó utasítások

Protocols

This procedure may be used for all Catalase products.

Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.

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