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para-Nitrophenylphosphate (pNPP) is a non-proteinaceous chromogenic substrate for alkaline and acid phosphatases used in ELISA and conventional spectrophotometric assays. [1] Phosphatases catalyze the hydrolysis of pNPP liberating inorganic phosphate and the conjugate base of para -nitrophenol (pNP).
The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase, also abbreviated PhoA) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found ...
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Alkaline phosphatase primarily hydrolyzes phosphate monoester bonds, but it shows some promiscuity towards hydrolyzing phosphate diester bonds, making it a sort of opposite to NPP. The active sites of these two enzymes show marked similarities, namely in the presence of nearly superimposable Zn 2+ bimetallo catalytic centers.
Other names in common use include nitrophenyl phosphatase, p-nitrophenylphosphatase, para-nitrophenyl phosphatase, K-pNPPase, NPPase, PNPPase, Ecto-p-nitrophenyl phosphatase, and p-nitrophenylphosphate phosphohydrolase. This enzyme participates in γ-hexachlorocyclohexane degradation.
Alkaline phosphatase, placental type is a membrane-bound glycosylated dimeric enzyme, also referred to as the heat-stable form, that is expressed primarily in the placenta, although it is closely related to the intestinal form of the enzyme as well as to the placental-like form.
5-Bromo-4-chloro-3-indolyl phosphate (BCIP, X-phosphate, XP) is an artificial chromogenic substrate used for the sensitive colorimetric detection of alkaline phosphatase activity. It is, for example, used in immunoblotting , in situ hybridization , and immunohistochemistry , often in combination with nitro blue tetrazolium chloride (NBT).
This type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate-based phosphatases. PP1 has been found to be important in the control of glycogen metabolism, muscle contraction , cell progression, neuronal activities, splicing of RNA , mitosis , [ 1 ] cell division, apoptosis , protein synthesis, and regulation of ...
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