P3895
Phosphatase, Alkaline from human placenta
≥10 units/mg solid (in glycine buffer)
Synonym(s):
Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
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About This Item
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form
solid
Quality Level
specific activity
≥10 units/mg solid (in glycine buffer)
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... ALPP(250)
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Application
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.
Biochem/physiol Actions
Alkaline phosphatase dephosphorylates proteins and nucleic acids. Human placental alkaline phosphatase (PLAP) has an unique residue, Glu-429. It is an allosteric enzyme that is uncompetitively inhibited by L-Phe, L-Trp, and L-Leu. PLAP is post-translationally modified. Phosphatidylinositol-specific phospholipase C may be involved in the release of PLAP. PLAP may have a role in cell division and may be involved in the transfer of maternal IgG to the fetus[1].
Unit Definition
One unit will hydrolyze 1 μmole of 4-nitrophenyl phosphate per minute at pH 10.4 at 37 °C.
inhibitor
Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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The Journal of biological chemistry, 276(12), 9158-9165 (2001-01-01)
Human placental alkaline phosphatase (PLAP) is one of three tissue-specific human APs extensively studied because of its ectopic expression in tumors. The crystal structure, determined at 1.8-A resolution, reveals that during evolution, only the overall features of the enzyme have
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