C9322
Catalase from bovine liver
lyophilized powder, 2,000-5,000 units/mg protein
Synonym(s):
H2O2:H2O2 oxidoreductase
Sign Into View Organizational & Contract Pricing
All Photos(4)
About This Item
Recommended Products
biological source
bovine liver
form
lyophilized powder
specific activity
2,000-5,000 units/mg protein
mol wt
tetramer ~250 kDa
isoelectric point
5.4
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
cow ... CAT(280743)
Looking for similar products? Visit Product Comparison Guide
General description
Research Area: Cell Signaling
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.
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.
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, catalzes 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.
Catalase from bovine liver may be used:
Catalase from bovine liver may be used:
- to prepare H2O2-O2 based biocathode for applications in glucose biofuel cells
- to study the kinetic properties and storage stability of catalase immobilized on to florisil
- in glutathione-mediated superoxide generation in an aqueous solution
Biochem/physiol Actions
Catalase, an antioxidant enzyme found in all aerobic organisms, catalyzes the degradation of hydrogen peroxide, a byproduct of metabolic processes, into less harmful 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. Catalase enzyme uses either iron (Fe) or manganese (Mn) as cofactor, and are classified as Fe-CAT or Mn-CAT.
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.
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.
The enzyme is soluble in 50 mM potassium phosphate buffer at 1 mg/mL and pH 7.0.
inhibitor
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
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)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
Articles
Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.
Protocols
This procedure may be used for all Catalase products.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service