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250 UNITS
295,00 zł
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Pozwól nam pomócrecombinant
expressed in E. coli
Quality Level
form
lyophilized powder
specific activity
≥70 units/mg protein
storage temp.
−20°C
1 of 4
Ta pozycja | |||
|---|---|---|---|
| specific activity ≥70 units/mg protein | specific activity ≥10 units/mg protein | specific activity ≥10 units/mg protein | specific activity ≥1300 U/mL |
| recombinant expressed in E. coli | recombinant expressed in E. coli | recombinant - | recombinant expressed in E. coli |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form liquid |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 100 |
General description
The roles of the residues in the catalytic active site of pyrimidine nucleoside phosphorylase from Bacillis subtilis have been elucidated using hybrid quantum-mechanical/molecular-mechanical methods.
Biochem/physiol Actions
Pyrimidine nucleoside phosphorylase functions in the nucleotide synthesis salvage pathway by catalyzing the reversible phosphorolysis of pyrimidines. Both uridine and thymidine are substrates.
Other Notes
One unit will convert 1 μmole each of 2′-deoxyuridine and phosphate to uracil and 2-deoxyribose 1-phosphate per minute at pH 7.4 and 37 °C.
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Klasa składowania
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Xue-Feng Gao et al.
Journal of structural biology, 154(1), 20-26 (2006-02-14)
Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide synthesis salvage pathway. We have built a model of a closed active conformation of the three-dimensional structure of PYNP from Bacillus subtilis. Using docking, molecular dynamics, and
A Danchin
DNA research : an international journal for rapid publication of reports on genes and genomes, 4(1), 9-18 (1997-02-28)
Genome comparison permits identification of chromosome regions conserved during evolution. Bacillus subtilis and Escherichia coli are so distant that there exists very few conserved landmarks in their genome organisation. Analysis of the conserved cmk rpsA cluster pinpointed the importance of
M J Pugmire et al.
Structure (London, England : 1993), 6(11), 1467-1479 (1998-11-18)
Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide synthesis salvage pathway. In lower organisms (e.g. Bacillus stearothermophilus) PYNP accepts both thymidine and uridine, whereas in mammalian and other higher organisms it is specific for thymidine
T Hamamoto et al.
Bioscience, biotechnology, and biochemistry, 60(7), 1179-1180 (1996-07-01)
The purine nucleoside phosphorylase (Pu-NPase) and the pyrimidine nucleoside phosphorylase (Py-NPase) have been purified from Bacillus stearothermophilus TH 6-2. The Pu-NPase is a trimer of 30-kDa subunits and the Py-NPase is a dimer of 46-kDa subunits. The isoelectric points of
K Okuyama et al.
Bioscience, biotechnology, and biochemistry, 60(10), 1655-1659 (1996-10-01)
The pyrimidine nucleoside phosphorylase (Py-NPase) of Bacillus stearothermophilus TH 6-2 is a dimer of 46-kDa subunits and catalyzes the reversible phosphorolysis of uridine and thymidine. The gene encoding this pyrimidine nucleoside phosphorylase (pyn gene) has been cloned and sequenced from
Numer pozycji handlu globalnego
| SKU | NUMER GTIN |
|---|---|
| N3665-1KU | 04061826691984 |
| N3665-250UN | 04061832924779 |
| N3665-5KU | 04061832924786 |
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