A2237
Phosphatase, Alkaline shrimp
≥900 DEA units/mL, buffered aqueous glycerol solution, recombinant, expressed in proprietary host
Synonym(s):
Phosphatase, Alkaline from shrimp, Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
recombinant
expressed in proprietary host
Quality Level
form
buffered aqueous glycerol solution
concentration
≥900 DEA units/mL
foreign activity
RNAse, DNAse, none detected
shipped in
dry ice
storage temp.
−20°C
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General description
Shrimp alkaline phosphatase is a heat labile, hydrolase enzyme. It is a high specific activity alkaline phosphatase purified from a recombinant source. There are two preferred sites for enzyme activity: 5′ protruding, recessive and blunt 5′-termini. The enzyme is irreversibly heat inactivated at 65°C for 15 minutes.
Application
Alkaline phosphatase was used to examine its role in the prevention of high-fat-diet-induced metabolic syndrome in mice. It also may be used in pasteurization process for milks used in dairy products.
Biochem/physiol Actions
Alkaline phosphatase is commonly responsible for dephosphorylation of nucleotides, proteins and alkaloids. The enzyme nonspecifically catalyzes the dephosphorylation of 5′-termini DNA and RNA phosphomonoesters reactions but it does not affect diphosphate or triphosphate linkages.
Physical form
solution in 50% glycerol containing 25 mM Tris-HCl, pH 7.5, 1 mM MgCl2
Analysis Note
Protein determined by biuret
Other Notes
One unit will hydrolyze 1 μmole of 4-nitrophenyl phosphate per minute at pH 9.8 at 37 °C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Nicoletta I Petridou et al.
Cell, 184(7), 1914-1928 (2021-03-18)
Embryo morphogenesis is impacted by dynamic changes in tissue material properties, which have been proposed to occur via processes akin to phase transitions (PTs). Here, we show that rigidity percolation provides a simple and robust theoretical framework to predict material/structural
Naomi Ofer et al.
The Journal of biological chemistry, 288(16), 11287-11293 (2013-03-09)
Protein degradation via prokaryotic ubiquitin-like protein (Pup) tagging is conserved in bacteria belonging to the phyla Actinobacteria and Nitrospira. The physiological role of this novel proteolytic pathway is not yet clear, although in Mycobacterium tuberculosis, the world's most threatening bacterial
Gouri Chaudhuri et al.
Indian journal of biochemistry & biophysics, 50(1), 64-71 (2013-04-27)
The hydrolysis of p-nitrophenyl phosphate (pNPP) by calf intestinal alkaline phosphatase (CIAP) was investigated with respect to kinetic parameters such as V(max), K(m) and K(cat) under varying pH, buffers, substrate concentration, temperature and period of incubation. Highest activity was obtained
George C Ziobro et al.
Journal of food protection, 76(5), 892-898 (2013-05-07)
Over the past 80 years, a variety of methods have been developed to detect underpasteurized or improperly pasteurized milks used in dairy products. Existing methods are hampered by duration of analysis, poor reproducibility, and in some cases the use of
I V Zverinskiĭ et al.
Biomeditsinskaia khimiia, 59(1), 90-96 (2013-05-09)
On the eighth day after ligation of the common bile duct in rats a significant increase in the serum content of total lipids, cholesterol bilirubin and ALT, alkaline phosphatase, and gamma-glutamyltransferase was observed. In the microsomal fraction there was a
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