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Alanin-Dehydrogenase, rekombinant
recombinant, expressed in E. coli, ≥15 U/mg
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10 MG
€ 131,00
50 MG
€ 490,00
€ 131,00
Voraussichtliches Versanddatum16. April 2025
Alle Fotos(1)
Größe auswählen
Ansicht ändern
10 MG
€ 131,00
50 MG
€ 490,00
About This Item
€ 131,00
Voraussichtliches Versanddatum16. April 2025
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Form
crystals
powder
Spezifische Aktivität
≥15 U/mg
Lagertemp.
−20°C
Anwendung
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. Wirkung
Alanine dehydrogenase catalyzes the reversible reductive amination of pyruvate using NADH as an oxidation/reduction cofactor [1].
Einheitendefinition
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).
Signalwort
Danger
H-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
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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
Wei Ye et al.
Microbiological research, 165(4), 268-275 (2009-09-02)
The major objective of the present study is to change the alanine production of Lactic acid bacteria by expression of Bacillus subtilis (natto) alanine dehydrogenase (AlaDH), the gene that is not present in Lactic acid. B. subtilis AlaDH gene (ald)
S Shafe et al.
The West Indian medical journal, 58(2), 164-172 (2009-01-01)
The present study sought to determine whether an association exists between alcohol dependence and select affective and anxiety disorders in patients presenting at substance abuse centres in Trinidad and Tobago (TT). The participants in this study were 143 alcohol dependents
Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations.
Sarvind Mani Tripathi et al.
Proteins, 72(3), 1089-1095 (2008-05-21)
Karin Denger et al.
Microbiology (Reading, England), 152(Pt 11), 3197-3206 (2006-11-01)
A degradative pathway for taurine (2-aminoethanesulfonate) in Rhodobacter sphaeroides 2.4.1 was proposed by Brüggemann et al. (2004) (Microbiology 150, 805-816) on the basis of a partial genome sequence. In the present study, R. sphaeroides 2.4.1 was found to grow exponentially
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