P5931
Phosphatase, Alkaline from Escherichia coli
lyophilized powder, 30-60 units/mg protein (in glycine buffer)
Sinônimo(s):
Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
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100 UNITS
R$ 2.142,00
200 UNITS
R$ 3.956,00
500 UNITS
R$ 8.561,00
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100 UNITS
R$ 2.142,00
200 UNITS
R$ 3.956,00
500 UNITS
R$ 8.561,00
About This Item
Produtos recomendados
Formulário
lyophilized powder
Nível de qualidade
atividade específica
30-60 units/mg protein (in glycine buffer)
composição
Protein, ~50% biuret
temperatura de armazenamento
−20°C
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Descrição geral
Alkaline phosphatase (ALP) of E.coli is a member of an enzyme group that possesses intragenic complementation.[1]
Aplicação
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].
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.[3]
Ações bioquímicas/fisiológicas
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[4][5][6]. E. coli akaline phosphatase has a broad specificity for phosphate esters[4].
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.[7][8][9] 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.
Definição da unidade
One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 10.4 at 37 °C.
forma física
Lyophilized powder containing Tris buffer salts, MgSO4, and ZnSO4
Nota de preparo
Chromatographically purified
Inibidor
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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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
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)
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
Alkaline phosphatase from Thermotoga neapolitana.
A Savchenko et al.
Methods in enzymology, 331, 298-305 (2001-03-27)
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