P8250
Peroxidase from horseradish
Type II, essentially salt-free, lyophilized powder, 150-250 units/mg solid (using pyrogallol)
Synonym(s):
Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase
Sign Into View Organizational & Contract Pricing
All Photos(6)
About This Item
Recommended Products
biological source
horseradish
Quality Level
type
Type II
form
essentially salt-free, lyophilized powder
specific activity
150-250 units/mg solid (using pyrogallol)
mol wt
~44 kDa
solubility
0.1 M phosphate buffer: soluble (pH 6.0)
H2O: soluble
absorbance ratio
RZ ≥1.8
application(s)
diagnostic assay manufacturing
storage temp.
2-8°C
SMILES string
[O+H2]O[O-]
InChI
1S/H2O3/c1-3-2/h1-2H
InChI key
JSPLKZUTYZBBKA-UHFFFAOYSA-N
Looking for similar products? Visit Product Comparison Guide
General description
Horseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.
Application
Horseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Horseradish peroxidase, product P8250, has been used to study nonoral antigens in inflamed gingiva and Ebola virus glycoprotein toxicity.
The enzyme has been used as a comparison during the peroxidase assay of extract from mature tall fescue leaf blades. It has also been used to measure H2O2 production.
Biochem/physiol Actions
HRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding. It is also used for the determination of glucose and peroxides in solution. Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, Pb2+ ions are found to inhibit the enzyme activity.
When incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.
Quality
Preliminary work shows it to contain at least five isoenzymes.
Unit Definition
One pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.
Analysis Note
The RZ (Reinheitszahl) is the absorbance ratio A403/A275 determined at 0.5-1.0 mg/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.
Other Notes
View more information on peroxidase at www.sigma-aldrich.com/enzymeexplorer.
inhibitor
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 1
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.
Customers Also Viewed
J W Macadam et al.
Plant physiology, 99(3), 872-878 (1992-07-01)
Cessation of cell expansion has been associated with cell wall cross-linking reactions catalyzed by peroxidase. This study utilized two genotypes of tall fescue (Festuca arundinacea Schreb.) that differ in length of the leaf elongation zone to investigate the relationship between
Chuan Chiang-Ni et al.
Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi, 49(6), 837-842 (2015-02-05)
The phenotypic heterogeneity of the human pathogen Streptococcus pyogenes [group A streptococcus (GAS)] is associated with bacterial virulence variation. During invasive GAS infection, mutations in the two-component regulatory system covR/covS leads to increases in hyaluronic acid capsule production, virulence genes
S M Mallison et al.
Infection and immunity, 56(4), 823-830 (1988-04-01)
In vitro experimentation indicates that periodontitis-associated bacteria contain potent polyclonal B-cell activators (PBA). We reasoned that if PBA were operative in vivo, plasma cells specific for nonoral antigens should be present in the inflamed gingival tissues, which are characterized by
W E Bullock et al.
The Journal of experimental medicine, 165(1), 195-210 (1987-01-01)
The principal host cell of H. capsulatum (Hc) is the M phi within which the pathogenic yeast phase of the fungus multiplies during active disease. The initial interaction between Hc yeasts and M phi therefore is a crucial step in
Nancy J Sullivan et al.
Journal of virology, 79(1), 547-553 (2004-12-15)
Ebola virus infection causes a highly lethal hemorrhagic fever syndrome associated with profound immunosuppression through its ability to induce widespread inflammation and cellular damage. Though GP, the viral envelope glycoprotein, mediates many of these effects, the molecular events that underlie
Related Content
Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.
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