P0114

One DEA unit will hydrolyze 1 micromole of 4-nitrophenyl phosphate per minute at pH 9.8 at 37 °C.

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P0114

Sigma

 

Phosphatase, Alkaline from bovine intestinal mucosa

BioUltra, buffered aqueous glycerol solution, ≥7,500 DEA units/mg protein

Synonym:Alkaline phosphatase, Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
CAS Number:9001-78-9
Enzyme Commission (EC) Number:3.1.3.1   ( BRENDA | IUBMB )
EC Number:232-631-4
MDL number:MFCD00131849

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Description

Analysis NotePackage sizes are based on DEA units
ApplicationHigh specific activity grade recommended for antibody and protein conjugation.
Biochem/physiol ActionsThe enzyme has a broad specificity for phosphate esters of alcohols, amines, pyrophosphate, and phenols. It is routinely used to dephosphorylate proteins and nucleic acids.
Unit DefinitionOne DEA unit will hydrolyze 1 μmole of 4-nitrophenyl phosphate per minute at pH 9.8 at 37 °C. (One glycine unit is equivalent to ~3 DEA units)
Physical formSolution in 50% glycerol containing 5 mM Tris, 5 mM MgCl2 and 0.1 mM ZnCl2, pH 7.0
 Alkaline phosphatase can be used to dephosphorylate casein and other proteins. Alkaline phosphatase may be also be used to dephosphorylate the 5'-termini of DNA or RNA to prevent self-ligation. DNA or RNA can also be tagged with radiolabeled phosphate (via T4 polynucleotide kinase) after dephosphorylation with alkaline phosphatase..
Physical propertiesBovine intestinal alkaline phosphatase is a dimeric, membrane-derived glycoprotein. At least three isoforms exist, which typically possess two N-linked and one or more O-linked glycans per monomer.2 The enzyme requires zinc, and magnesium or calcium divalent ions for activity.

Properties

gradeBioUltra
formbuffered aqueous glycerol solution
mol wthomodimer mol wt ~160 kDa
storage temp.2-8°C

References

referenceReid, T.W., et al. Enzymes 3, 373-416, (1971)
 Takanami, M., Analysis of the 5'-terminal nucleotide sequences of ribonucleic acids 1. the 5'-termini of Escherichia coli ribosomal RNA. J. Mol. Biol. 23, 135, (1967)