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A propos de cet article
Numéro CAS:
eCl@ss:
42010102
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-630-9
MDL number:
Specific activity:
≥3.0 units/mg solid
Service technique
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lyophilized powder
Quality Level
specific activity
≥3.0 units/mg solid
mol wt
69 kDa
shipped in
wet ice
storage temp.
−20°C
SMILES string
O(CC(O)C)CC#C
InChI
1S/C6H10O2/c1-3-4-8-5-6(2)7/h1,6-7H,4-5H2,2H3
InChI key
GZCWLCBFPRFLKL-UHFFFAOYSA-N
General description
Acid phosphatase from potato is a phosphomonoesterase, which can appear in multiple molecular forms of similar molecular mass but with different isoelectric points.
Application
Acid phosphatase from potato has been used in a study to assess the potential allergenicity of novel gene products. It has also been used in a study to remove eight phosphate groups from casein at a pH of 7.0.
The activity of potato acid phosphatase in various surfactant medias was examined. Bis(2- ethylhexyl)sodium sulfosuccinate, Brij 35, and SDS at 3mM inhibited phosphatase activity while the surfactant cetyltrimethylammonium bromide enhanced activity.
Biochem/physiol Actions
Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7.
Other Notes
One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 4.8 at 37 °C.
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Contenu apparenté
J Lalitha et al.
Biochemistry and molecular biology international, 41(4), 797-803 (1997-04-01)
The effect of three different classes of surfactants viz., anionic, cationic and neutral on catalytic activity of potato acid phosphatase (AcPase) was studied. Anionic surfactants bis(2-ethylhexyl) sodium sulfosuccinate (AOT) and sodium dodecyl sulfate (SDS) inhibited AcPase activity completely at 3
Mariusz Olczak et al.
Acta biochimica Polonica, 50(4), 1245-1256 (2004-01-24)
The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal ligation. Animal PAPs contain a binuclear
Y Sugiura et al.
The Journal of biological chemistry, 256(20), 10664-10670 (1981-10-25)
A new manganese-containing acid phosphatase has been isolated and crystallized from sweet potato tubers. The pure enzyme contains one atom of manganese per Mr = 110,000 polypeptide and shows phosphatase activity toward various phosphate substrates. The pH optimum of the
