P7640
Phosphatase, Alkaline from bovine intestinal mucosa
lyophilized powder, ≥10 DEA units/mg solid
Synonym(s):
Alkaline phosphatase, Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
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About This Item
Recommended Products
biological source
bovine intestinal mucosa
Quality Level
form
lyophilized powder
specific activity
≥10 DEA units/mg solid
mol wt
dimer ~160 kDa
shipped in
wet ice
storage temp.
−20°C
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Application
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..
Alkaline phosphatase is used for conjugation to antibodies and other proteins for ELISA, Western blotting, and histochemical detection. It is routinely used to dephosphorylate proteins and nucleic acids. It may be used for protein labeling when high sensitivity is required. 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.. Product P7640 has been used to study the monoclonal alkaline phosphatase-anti-alkaline phosphatase (APAAP) complex.
High specific activity grade recommended for antibody and protein conjugation.
Biochem/physiol Actions
Alkaline phosphatase, from bovine intestinal mucosa, is most stable in the pH range 7.5-9.5. The enzyme has a broad specificity for phosphate esters of alcohols, amines, pyrophosphate, and phenols and it requires zinc, and magnesium or calcium divalent ions for activity.
The enzyme has a broad specificity for phosphate esters of alcohols, amines, pyrophosphate, and phenols. It is routinely used to dephosphorylate proteins and nucleic acids.
Physical properties
Bovine 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.
Bovine 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.
Unit Definition
One 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)
Analysis Note
Package sizes are based on DEA units
inhibitor
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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A Hohmann et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 36(2), 137-143 (1988-02-01)
A mouse monoclonal antibody, FMC55 (an IgG1), to alkaline phosphatase was prepared and evaluated in immunostaining. Clones producing antibody to alkaline phosphatase were selected using a micro-ELISA which identified antibodies forming active soluble complexes (APAAP) with the enzyme. Conditions that
Simultaneous flow-injection determination of fluoride, monofluorophosphate and orthophosphate ions using alkaline phosphatase immobilized on a cellulose nitrate membrane and an open-circulation approach.
Tzanavaras PD and Themelis DG
Analytica Chimica Acta, 467 (1-2), 83-89 (2002)
Mamoni Dash et al.
Carbohydrate polymers, 182, 254-264 (2017-12-28)
Polyelectrolyte complexes (PEC) of chitosan and ulvan were fabricated to study alkaline phosphatase (ALP) mediated formation of apatitic minerals. Scaffolds of the PEC were subjected to ALP and successful mineral formation was studied using SEM, Raman and XRD techniques. Investigation
Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivity.
D Chappelet-Tordo et al.
Biochemistry, 13(9), 1788-1795 (1974-04-23)
On the mechanism of inhibition of intestinal alkaline phosphatase by L-phenylalanine. I. Kinetic studies.
N K Ghosh et al.
The Journal of biological chemistry, 241(11), 2516-2522 (1966-06-10)
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