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MilliporeSigma

10108090001

Roche

Peroxidase (POD)

grade I, from horseradish

Synonym(s):

POD, peroxidase

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25000 UNITS

$431.00

$431.00

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About This Item

UNSPSC Code:
12352204
EC Number:
1.11.1.7 (BRENDA, IUBMB)
NACRES:
NA.54
Specific activity:
≥250 units/mg protein (At 25 °C with guaiacol and H2O2 as the substrates.), 250 U/mg
Biological source:
horseradish

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biological source

horseradish

form

lyophilized (salt-free)

specific activity

≥250 units/mg protein (At 25 °C with guaiacol and H2O2 as the substrates.), 250 U/mg

packaging

pkg of 25,000 U

manufacturer/tradename

Roche

optimum pH

6.0-6.5

shipped in

wet ice

storage temp.

2-8°C

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This Item
1142886100110814407001SRE0082
Peroxidase (POD) grade I, from horseradish

Roche

10108090001

Peroxidase (POD)

Peroxidase (POD), activated from horseradish

Roche

11428861001

Peroxidase (POD), activated

Peroxidase (POD) EIA grade, from horseradish

Roche

10814407001

Peroxidase (POD)

Peroxidase from horseradish For research or further manufacturing use only. Not intended for direct use in humans or animals. Non-TSCA use only in US, Type VI, powder, stabilized, ≥250 units/mg solid (using pyrogallol)

Sigma-Aldrich

SRE0082

Peroxidase from horseradish

biological source

horseradish

biological source

horseradish

biological source

horseradish

biological source

-

specific activity

≥250 units/mg protein (At 25 °C with guaiacol and H2O2 as the substrates.), 250 U/mg

specific activity

800 units/mg protein (at 25 °C with ABTS and H2O2 as substrate (pH 5.0).)

specific activity

~225 U/mg lyophilizate, 25 °C (Guaiacol, H2O2)

specific activity

≥250 units/mg solid (using pyrogallol)

form

lyophilized (salt-free)

form

lyophilized

form

lyophilized (salt-free)

form

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C (−15°C to −25°C)

storage temp.

2-8°C

shipped in

wet ice

shipped in

wet ice

shipped in

dry ice

shipped in

wet ice

optimum pH

6.0-6.5

optimum pH

6.0-6.5

optimum pH

6.0-6.5

optimum pH

-

General description

Donor:hydrogen-peroxide oxidoreductase
Peroxidase (POD) (E.C. 1.11.1.7) is extensively expressed in most fruits and vegetables.[1]

Application

Oxidation of electron donors (e.g., epoxidation of double bonds). Peroxidase can be coupled to other proteins via its amino groups, as well as its carbohydrate moiety. The reconstituted solution can be used directly for conjugation without prior dialysis.It has been used in ligand blotting.[2]
Peroxidase (POD) has been used in AUR (Amplex UltraRed assay) to measure extracellular H2O2 produced from disaggregated slug cells.[3]

Biochem/physiol Actions

Peroxidase (POD) is involved in the dehydrogenation of a large number of organic compounds including, phenols and aromatic amines, hydroquinones and hydroquinoid amines, mainly benzidine derivatives.[4]

Preparation Note

Activator: Ammonia, pyridine, imidazole, all at pH >7; detergents.
Working solution: PBS (phosphate buffered saline) or water (starting concentration 20 mg/ml).
Solution (10 mg/ml in water): clear, red brown; pH-value: 6.0 to 7.0.

Analysis Note

Contaminants: <0.001% ATPase and acid phosphatase each, <0.7% catalase
Purity number: approximately 3.0 (A403/A275)

Other Notes

For life science research only. Not for use in diagnostic procedures.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
63787428
57537735
39428322
14191224
14191223

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Inactivation and conformational change of horseradish peroxidase induced by pulsed electric field
Zhong K, et al.
Food Chemistry, 92(3), 473-479 (2005)
Mi Kyong Lee et al.
Applied and environmental microbiology, 69(8), 4648-4657 (2003-08-07)
The Vip3A protein, secreted by Bacillus spp. during the vegetative stage of growth, represents a new family of insecticidal proteins. In our investigation of the mode of action of Vip3A, the 88-kDa Vip3A full-length toxin (Vip3A-F) was proteolytically activated to
Social amoebae trap and kill bacteria by casting DNA nets
Zhang X, et al.
Nature Communications, 7, 10938-10938 (2016)
Methods of Enzymatic Analysis (1974)
Xuezhi Zhang et al.
Nature communications, 7, 10938-10938 (2016-03-02)
Extracellular traps (ETs) from neutrophils are reticulated nets of DNA decorated with anti-microbial granules, and are capable of trapping and killing extracellular pathogens. Various phagocytes of mammals and invertebrates produce ETs, however, the evolutionary history of this DNA-based host defence

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