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Peroxidase from horseradish

Name: Peroxidase from horseradish
Brand: SIGMA

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

Synonym(s):

Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase

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About This Item

CAS Number:

9003-99-0

eCl@ss:

32160410

UNSPSC Code:

12352204

NACRES:

NA.54

EC Number:

232-668-6

MDL number:

MFCD00071339

EC Number:

1.11.1.7 (BRENDA, IUBMB)

Specific activity:

150-250 units/mg solid (using pyrogallol)

Biological source:

horseradish

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biological source

horseradish

Quality Level

300

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

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This Item	P8375	P6782	SRE0082
Sigma-Aldrich P8250 Peroxidase from horseradish	Sigma-Aldrich P8375 Peroxidase from horseradish	Sigma-Aldrich P6782 Peroxidase from horseradish	Sigma-Aldrich SRE0082 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 ≥250 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 powder, stabilized
application(s) diagnostic assay manufacturing	application(s) diagnostic assay manufacturing	application(s) diagnostic assay manufacturing	application(s) diagnostic assay manufacturing
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 phosphate buffer: soluble
mol wt ~44 kDa	mol wt ~44 kDa	mol wt ~44 kDa	mol wt -

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.

pictograms

GHS08

signalword

Danger

hcodes

H334

pcodes

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class

13 - Non Combustible Solids

ppe

Eyeshields, Gloves, type N95 (US)

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Antibody synthesis specific for nonoral antigens in inflamed gingiva.

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

Peroxidase activity in the leaf elongation zone of tall fescue : I. Spatial distribution of ionically bound peroxidase activity in genotypes differing in length of the elongation zone.

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

Role of the adherence-promoting receptors, CR3, LFA-1, and p150,95, in binding of Histoplasma capsulatum by human macrophages.

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

Oxygen-dependent phenotypic variation in group A streptococcus.

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

Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent protein-trafficking pathway.

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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Global Trade Item Number

SKU	GTIN
P8250-200KU	04061834401216
P8250-25KU	04061834401223
P8250-100KU	04061834401209
P8250-5KU	04061835558773
P8250-500KU	04065265034562
P8250-50KU	04061835513017

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