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Merck

A2237

Sigma-Aldrich

Phosphatase, Alkaline shrimp

≥900 DEA units/mL, buffered aqueous glycerol solution, recombinant, expressed in proprietary host

Sinónimos:

Phosphatase, Alkaline from shrimp, Orthophosphoric-monoester phosphohydrolase (alkaline optimum)

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About This Item

Número de CAS:
Comisión internacional de enzimas:
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.

Unit Definition

One unit will hydrolyze 1 μmole of 4-nitrophenyl phosphate per minute at pH 9.8 at 37 °C.

Physical form

solution in 50% glycerol containing 25 mM Tris-HCl, pH 7.5, 1 mM MgCl2

Analysis Note

Protein determined by biuret

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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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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