P7383
Pyrophosphatase, Nucleotide from Crotalus adamanteus venom
Type II, lyophilized powder, 4-8 units/mg protein, vial of ~25 units
Synonym(s):
Dinucleotide nucleotidohydrolase
type
Type II
form
lyophilized powder
specific activity
4-8 units/mg protein
packaging
vial of ~25 units
foreign activity
5′-nucleotidase <0.003 units/mg protein, alkaline phosphatase <0.002 units/mg protein, phosphodiesterase 0.2 - 0.4 units/mg protein
storage temp.
−20°C
Physical form
Lyophilized powder containing approx. 35% Tris buffer salts.
Other Notes
One unit will hydrolyze 1.0 μmole of β-NAD to NMN and AMP per min at pH 7.4 at 37 °C in the presence of Mg ions.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Eileen J Kennedy et al.
Eukaryotic cell, 4(11), 1892-1901 (2005-11-10)
Extracellular nucleotides play many biological roles, including intercellular communication and modulation of nucleotide receptor signaling, and are dependent on the phosphorylation state of the nucleotide. Regulation of nucleotide phosphorylation is necessary, and a specialized class of enzymes, nucleotide pyrophosphatases/phosphodiesterases (E-NPPs)
Zhongqi He et al.
Bioresource technology, 97(14), 1660-1668 (2005-09-13)
Characterizing labile P forms in animal manure is a challenge due to their susceptibility to hydrolysis. In this study, we enzymatically characterized P forms in dairy manure (no bedding), collected from a representative dairy farm in New York, by separating
Gennady G Yegutkin et al.
The Journal of physiology, 579(Pt 2), 553-564 (2007-01-06)
Extracellular ATP and ADP trigger vasodilatatory and prothrombotic signalling events in the vasculature. Here, we tested the hypothesis that nucleotide turnover is activated in the bloodstream of exercising humans thus contributing to the enhanced platelet reactivity and haemostasis. Right atrial
Ildikó Pécsi et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(35), 14437-14442 (2011-08-13)
We investigated the potential (d)NDP/(d)NTP discrimination mechanisms in nucleotide pyrophosphatases. Here, we report that dUTPase, an essential nucleotide pyrophosphatase, uses a C-terminal P-loop-like sequence in a unique mechanism for substrate discrimination and efficient hydrolysis. Our spectroscopy and transient kinetics results
Iris J Joye et al.
Applied microbiology and biotechnology, 90(1), 173-180 (2010-12-31)
Nucleotide pyrophosphatases/phosphodiesterases (NPPs, PF01663) release nucleoside 5'-monophosphates from a wide range of nucleotide substrates. Only very recently, the first plant members of the NPP family were characterised (Joye et al. J Cereal Sci 51: 326-336, 2010), and little is known
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