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P5931

Phosphatase, Alkaline from Escherichia coli

lyophilized powder, 30-60 units/mg protein (in glycine buffer)

Synonim(y):

Orthophosphoric-monoester phosphohydrolase (alkaline optimum)

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100 UNITS

1210,00 zł

200 UNITS

2230,00 zł

500 UNITS

15 780,00 zł

1210,00 zł


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Informacje o tej pozycji

Numer CAS:
UNSPSC Code:
12352204
eCl@ss:
42010105
EC Number:
232-631-4
NACRES:
NA.54
MDL number:
Numer WE:
Specific activity:
30-60 units/mg protein (in glycine buffer)

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form

lyophilized powder

specific activity

30-60 units/mg protein (in glycine buffer)

composition

Protein, ~50% biuret

storage temp.

−20°C

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Ta pozycja
P4252P0114P5521
specific activity

30-60 units/mg protein (in glycine buffer)

specific activity

30-90 units/mg protein (modified Warburg-Christian, in glycine buffer)

specific activity

≥5,700 DEA units/mg protein

specific activity

≥2,000 DEA units/mg protein

form

lyophilized powder

form

ammonium sulfate suspension

form

(40% glycerol containing 6 mM Tris, 6 mM MgCl2 and 0.12 mM ZnCl2, pH approximately 7.6)

form

aqueous solution

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

200

composition

Protein, ~50% biuret

composition

-

composition

-

composition

-

General description

Alkaline phosphatase (ALP) of E.coli is a member of an enzyme group that possesses intragenic complementation.

Application

The enzyme from Sigma has been used to develop a synthetic nanopore membrane. This membrane mimics protein channels that are regulated by phosphorylation/dephosphorylation and uses an aligned array of carbon nanotubes (CNTs) impregnated in a polystyrene matrix.[1]
Alkaline phosphatase is used for conjugation to antibodies and other proteins for ELISA, Western blotting, and histochemical detection. It may be used for protein labeling when high sensitivity is required. Product P5931 has been used during immunoblots to treat cell membranes prior to Tau1 incubation[2].

Biochem/physiol Actions

Alkaline phosphatase, from Escherichia coli, is a dimeric, non-glycosylated protein which mainly reside in the periplasmic space. Three known isoforms exist. The enzyme requires zinc, and is activated by magnesium[3][4]. E. coli akaline phosphatase has a broad specificity for phosphate esters.
The enzyme is a phosphohydrolase having an optimal pH of 10 in vitro. The actual optimum pH varies depending on the nature and concentration of the substrate, the type of buffer, the phosphate acceptor, and to some extent the nature of the isoenzymes. It catalyzes the hydrolysis of phosphate monoesters such as p-nitrophenyl phosphate, phenyl phosphate, phenolphthalein phosphate, α-glycerol phosphate, β-glycerol phosphate, 2-phosphorylglycerate, triosephosphate, glucose-6-phosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, adenosine 5-phosphate adenosine 3-phosphate, phosphoenolpyruvate, and β-nicotinamide adenine dinucleotide phosphate.[5][6][7] The activity is inhibited by 1,10-phenanthroline monohydrate, diethylenetriaminepentaacetic acid, ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid, and ethylenediaminetetraacetic acid disodium salt dihydrate.

Physical form

Lyophilized powder containing Tris buffer salts, MgSO4, and ZnSO4

Preparation Note

Chromatographically purified

Other Notes

One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 10.4 at 37 °C.
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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Klasa składowania

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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

Odwiedź Bibliotekę dokumentów

1.Reid, T., and Wilson
E. coli Alkaline Phosphatase,The Enzymes, 3rd Ed. Vol. 4, 4, 373-373 (1971)
Characterization of Heterodimeric Alkaline Phosphatases from Escherichia coli: An Investigation of Intragenic Complementation
Hehir MJ, et al.
Journal of molecular biology, 304(4), 645-656 (2000)
Alkaline phosphatase from Thermotoga neapolitana.
A Savchenko et al.
Methods in enzymology, 331, 298-305 (2001-03-27)
Sergey Korshunov et al.
Molecular microbiology, 113(1), 22-39 (2019-10-16)
The structure of free cysteine makes it vulnerable to oxidation by molecular oxygen; consequently, organisms that live in oxic habitats have acquired the ability to import cystine as a sulfur source. We show that cystine imported into Escherichia coli can
A Takeda et al.
The Journal of biological chemistry, 275(8), 5395-5399 (2000-02-22)
Increased expression of heme oxygenase-1 (HO-1) is a common feature in a number of neurodegenerative diseases. Interestingly, the spatial distribution of HO-1 expression in diseased brain is essentially identical to that of pathological expression of tau. In this study, we

Numer pozycji handlu globalnego

SKUNUMER GTIN
P5931-100UN04061834392637
P5931-500UN04061832759111
P5931-200UN04061834392644

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