73063
Alanine Dehydrogenase, recombinant
recombinant, expressed in E. coli, ≥15 U/mg
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10 MG
690,00 zł
50 MG
2540,00 zł
690,00 zł
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Informacje o tej pozycji
Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
Specific activity:
≥15 U/mg
Recombinant:
expressed in E. coli
Przejdź do
Pomoc techniczna
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Pozwól nam pomócrecombinant
expressed in E. coli
form
crystals, powder
specific activity
≥15 U/mg
storage temp.
−20°C
Quality Level
1 of 4
Ta pozycja | 59747 | 55689 | 43388 |
|---|---|---|---|
| specific activity ≥15 U/mg | specific activity ≥90 U/mg | specific activity ≥0.5 U/mg | specific activity ≥30.0 U/g |
| form crystals, powder | form powder | form lyophilized powder | form crystalline, crystals, powder or flakes |
| recombinant expressed in E. coli | recombinant expressed in E. coli | recombinant expressed in E. coli | recombinant expressed in E. coli |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| Quality Level 100 | Quality Level 100 | Quality Level 100 | Quality Level 100 |
Application
Alanine dehydrogenase (ald) is an oxidoreductase that is involved in taurin/hypotaurine metabolism and CO2 fixation. It is used in various enzyme assays and in kinetic studies [1].
Biochem/physiol Actions
Alanine dehydrogenase catalyzes the reversible reductive amination of pyruvate using NADH as an oxidation/reduction cofactor [1].
Other Notes
1 U corresponds to the amount of enzyme which converts 1 μmol L-alanine per minute at pH 10.0 and 30°C (NAD as cofactor).
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signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1
Klasa składowania
11 - Combustible Solids
wgk
WGK 3
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
M T Smith et al.
The Journal of biological chemistry, 268(15), 10746-10753 (1993-05-25)
The kinetic mechanism of alanine dehydrogenase from soybean nodule bacteroids was studied by initial velocity experiments with or without product inhibitors, dead-end inhibitors, or alternate substrates. Without inhibitors, double-reciprocal plots of initial velocity experiments showed intersecting lines, indicating a sequential
Sivagamisundaram Chavadi et al.
Journal of bacteriology, 191(24), 7545-7553 (2009-10-13)
To better understand the global effects of "natural" lesions in genes involved in the pyruvate metabolism in Mycobacterium bovis, null mutations were made in the Mycobacterium tuberculosis H37Rv ald and pykA genes to mimic the M. bovis situation. Like M.
Daniel Agren et al.
Journal of molecular biology, 377(4), 1161-1173 (2008-02-29)
L-alanine dehydrogenase from Mycobacterium tuberculosis catalyzes the NADH-dependent reversible conversion of pyruvate and ammonia to L-alanine. Expression of the gene coding for this enzyme is up-regulated in the persistent phase of the organism, and alanine dehydrogenase is therefore a potential
Roxane Lahmi et al.
Journal of bacteriology, 188(14), 5258-5265 (2006-07-04)
Degradation of the cyanobacterial light-harvesting antenna, the phycobilisome, is a general acclimation response that is observed under various stress conditions. In this study we identified a novel mutant of Synechococcus elongatus PCC 7942 that exhibits impaired phycobilisome degradation specifically during
A Sinem Ozyurt et al.
Proteins, 72(1), 184-196 (2008-01-25)
This study describes a method to computationally assess the function of homologous enzymes through small molecule binding interaction energy. Three experimentally determined X-ray structures and four enzyme models from ornithine cyclo-deaminase, alanine dehydrogenase, and mu-crystallin were used in combination with
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