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C9322

Sigma-Aldrich

Catalase from bovine liver

lyophilized powder, 2,000-5,000 units/mg protein

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Synonym(s):
H2O2:H2O2 oxidoreductase
CAS Number:
9001-05-2
Enzyme Commission number:
1.11.1.6 (BRENDA, IUBMB)
EC Number:
232-577-1
MDL number:
MFCD00081483
eCl@ss:
32160410
NACRES:
NA.54

biological source

bovine liver

Quality Level

400

form

lyophilized powder

specific activity

2,000-5,000 units/mg protein

mol wt

tetramer ~250 kDa

isoelectric point

5.4

UniProt accession no.

P00432

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

cow ... CAT(280743)

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Application

Catalase acts as a natural antioxidant to study the roles of reactive oxygen species in gene expression and apoptosis. It has also been used to protect against oxidative damage to proteins, lipids, and nucleic acids. Industrially, catalses have been used to remove hydrogen peroxide added to milk and cheese, in textile bleaching, and to examine its positive effects on the viability of DNA-repair mutants of E. coli.

Biochem/physiol Actions

This product doesn′t need any activators, but it is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogens bromide, 2-mercaptoethanol, dithiothreitol, dianisidnie and nitrate.
Catalase catalyzes the degradation of hydrogen peroxide into water and oxygen. It can also react with alkylhydrogen peroxides, such as methylperoxide and ethylperoxide and the second H2O2 molecule can be replaced by methanol, ethanol, propanol, formate and nitrate as a hydrogen donor.

Components

Catalase from bovine liver is a tetramer consisting of 4 equal subunits each with a 60 kDa molecular weight. Each of these subunits contains iron bound to a protoheme IX group. The enzyme will also strongly bind to NADP, where NADP and the heme group are within 13.7 angstroms.

Caution

Solutions of catalse should not be frozen. Frozen solution will result in a 50-70% loss of activity.

Unit Definition

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.

Preparation Note

This product is a lyophilized powder with activity of 2,000-5,000 units/mg.
The enzyme is soluble in 50 mM potassium phosphate buffer at 1 mg/mL and pH 7.0.

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How can Catalase from bovine liver, Product C9322, be reconstituted?

    This product is soluble in 50 mM potassium phosphate, pH 7.0 at a concentration of 10 mg/mL.

  4. How can a stock solution of Catalase from bovine liver, Product C9322, be stored?

    A 10 mg/mL stock solution prepared in 50 mM potassium phosphate, pH 7.0 and 50% glycerol was stable for at least 1 week in the freezer at -20°C.

  5. What salts are present in Catalase from bovine liver, Product C9322?

    Catalase (C9322) contains potassium phosphate buffered salts (and 20% trehalose as a stabilizer).

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Christopher Gell et al.
Methods in cell biology, 95, 221-245 (2010-05-15)
In vitro assays that reconstitute the dynamic behavior of microtubules provide insight into the roles of microtubule-associated proteins (MAPs) in regulating the growth, shrinkage, and catastrophe of microtubules. The use of total internal reflection fluorescence microscopy with fluorescently labeled tubulin
James C Dooley et al.
Current biology : CB, 30(12), 2404-2410 (2020-05-16)
Cortical development is an activity-dependent process [1-3]. Regarding the role of activity in the developing somatosensory cortex, one persistent debate concerns the importance of sensory feedback from self-generated movements. Specifically, recent studies claim that cortical activity is generated intrinsically, independent
Julie Elizabeth Keeble et al.
Pain, 141(1-2), 135-142 (2008-12-09)
Inflammatory diseases associated with pain are often difficult to treat in the clinic due to insufficient understanding of the nociceptive pathways involved. Recently, there has been considerable interest in the role of reactive oxygen species (ROS) in inflammatory disease, but
Eduard N Lavrentyev et al.
American journal of physiology. Heart and circulatory physiology, 296(1), H106-H118 (2008-11-04)
In rat diabetic animal models, ANG(1-7) treatment prevents the development of cardiovascular complications. Angiotensin-converting enzyme (ACE)2 is a major ANG(1-7)-generating enzyme in vascular smooth muscle cells (VSMCs), and its expression is decreased by a prolonged exposure to high glucose (HG)
Amol Aher et al.
Developmental cell, 46(1), 40-58 (2018-06-26)
The dynamic instability of microtubules plays a key role in controlling their organization and function, but the cellular mechanisms regulating this process are poorly understood. Here, we show that cytoplasmic linker-associated proteins (CLASPs) suppress transitions from microtubule growth to shortening
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Articles

Mitochondrial Stress and ROS

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.

Protocols

Enzymatic Assay of Catalase (EC 1.11.1.6)

This procedure may be used for all Catalase products.

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