P6772
Phosphatase, Alkaline from bovine intestinal mucosa
lyophilized powder, ≥2,000 DEA units/mg protein
Synonym(s):
Alkaline phosphatase, Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-631-4
MDL number:
form
lyophilized powder
specific activity
≥2,000 DEA units/mg protein
mol wt
dimer ~160 kDa
composition
Protein, 25-45% biuret
storage temp.
−20°C
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General description
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.
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..
High specific activity grade recommended for antibody and protein conjugation.
Biochem/physiol Actions
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 form
Lyophilized powder containing Tris-Citrate buffer salts
Preparation Note
Affinity purified. Prepared from P5521, Type VII-S.
Analysis Note
Package sizes are based on DEA units
Other Notes
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)
Storage Class
13 - Non 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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L Lizana et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(11), 4099-4104 (2008-03-14)
In biological systems, chemical activity takes place in micrometer- and nanometer-sized compartments that constantly change in shape and volume. These ever-changing cellular compartments embed chemical reactions, and we demonstrate that the rates of such incorporated reactions are directly affected by
A D Bakker et al.
Journal of dental research, 93(4), 394-399 (2014-02-05)
Mechanosensitive osteocytes regulate bone mass in adults. Interleukin 6 (IL-6), such as present during orthodontic tooth movement, also strongly affects bone mass, but little is known about the effect of IL-6 on osteocyte function. Therefore we aimed to determine in
M D McKee et al.
Journal of dental research, 92(8), 721-727 (2013-05-23)
Phosphatases are involved in bone and tooth mineralization, but their mechanisms of action are not completely understood. Tissue-nonspecific alkaline phosphatase (TNAP, ALPL) regulates inhibitory extracellular pyrophosphate through its pyrophosphatase activity to control mineral propagation in the matrix; mice without TNAP
Hanghang Huang et al.
The EMBO journal, 34(2), 154-168 (2014-12-04)
Autophagy is a catabolic process conserved among eukaryotes. Under nutrient starvation, a portion of the cytoplasm is non-selectively sequestered into autophagosomes. Consequently, ribosomes are delivered to the vacuole/lysosome for destruction, but the precise mechanism of autophagic RNA degradation and its
Jong Kil Lee et al.
The Journal of experimental medicine, 211(8), 1551-1570 (2014-07-23)
In Alzheimer's disease (AD), abnormal sphingolipid metabolism has been reported, although the pathogenic consequences of these changes have not been fully characterized. We show that acid sphingomyelinase (ASM) is increased in fibroblasts, brain, and/or plasma from patients with AD and
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