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Merck

P8250

Peroxidase from horseradish

Type II, essentially salt-free, lyophilized powder, 150-250 units/mg solid (using pyrogallol)

Synonim(y):

Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase

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Informacje o tej pozycji

Numer CAS:
9003-99-0
eCl@ss:
32160410
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-668-6
MDL number:
MFCD00071339
Numer WE:
1.11.1.7 (BRENDA, IUBMB)
Specific activity:
150-250 units/mg solid (using pyrogallol)
Biological source:
horseradish

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SMILES string

[O+H2]O[O-]

InChI key

JSPLKZUTYZBBKA-UHFFFAOYSA-N

InChI

1S/H2O3/c1-3-2/h1-2H

biological source

horseradish

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

Quality Level

300

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Ta pozycja
P8375P6782P8125
Peroxidase from horseradish Type II, essentially salt-free, lyophilized powder, 150-250 units/mg solid (using pyrogallol)

Sigma-Aldrich

P8250

Peroxidase from horseradish

Peroxidase from horseradish Type VI, essentially salt-free, lyophilized powder, ≥250 units/mg solid (using pyrogallol)

Sigma-Aldrich

P8375

Peroxidase from horseradish

Peroxidase from horseradish Type VI-A, essentially salt-free, lyophilized powder, 950-2000 units/mg solid (using ABTS), ≥250 units/mg solid (using pyrogallol)

Sigma-Aldrich

P6782

Peroxidase from horseradish

Peroxidase from horseradish Type I, essentially salt-free, lyophilized powder, ≥50 units/mg solid (using pyrogallol)

Sigma-Aldrich

P8125

Peroxidase from horseradish

specific activity

150-250 units/mg solid (using pyrogallol)

specific activity

≥250 units/mg solid (using pyrogallol)

specific activity

≥250 units/mg solid (using pyrogallol), 950-2000 units/mg solid (using ABTS)

specific activity

≥50 units/mg solid (using pyrogallol)

biological source

horseradish

biological source

-

biological source

-

biological source

-

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

solubility

0.1 M phosphate buffer: soluble (pH 6.0), H2O: soluble

solubility

0.1 M phosphate buffer: soluble 10 mg/mL, clear, orange to red (pH 6.0)

solubility

0.1 M phosphate buffer: soluble 10 mg/mL, clear, orange to red (pH 6.0), H2O: soluble

solubility

0.1 M phosphate buffer: soluble (pH 6.0), H2O: soluble

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

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[1] and Ebola virus glycoprotein toxicity[2].
The enzyme has been used as a comparison during the peroxidase assay of extract from mature tall fescue leaf blades.[3] It has also been used to measure H2O2 production.[4]

Biochem/physiol Actions

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.
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.

Analysis Note

Preliminary work shows it to contain at least five isoenzymes.
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

One pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.
View more information on peroxidase at www.sigma-aldrich.com/enzymeexplorer.
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pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Klasa składowania

13 - Non Combustible Solids

ppe

Eyeshields, Gloves, type N95 (US)

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Certyfikaty analizy (CoA)

Lot/Batch Number
0000523711
0000523711
0000508599
0000508587
0000508587

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
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
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
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