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Merck

73063

Sigma-Aldrich

Alanine Dehydrogenase, recombinant

recombinant, expressed in E. coli, ≥15 U/mg

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About This Item

Numer CAS:
Numer EC enzymu:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54

rekombinowane

expressed in E. coli

Poziom jakości

Postać

crystals
powder

aktywność właściwa

≥15 U/mg

temp. przechowywania

−20°C

Zastosowanie

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 .

Działania biochem./fizjol.

Alanine dehydrogenase catalyzes the reversible reductive amination of pyruvate using NADH as an oxidation/reduction cofactor .

Definicja jednostki

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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Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę 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
Xueli Zhang et al.
Applied microbiology and biotechnology, 77(2), 355-366 (2007-09-18)
Escherichia coli W was genetically engineered to produce L: -alanine as the primary fermentation product from sugars by replacing the native D: -lactate dehydrogenase of E. coli SZ194 with alanine dehydrogenase from Geobacillus stearothermophilus. As a result, the heterologous alanine
Toru Jojima et al.
Applied microbiology and biotechnology, 87(1), 159-165 (2010-03-11)
Corynebacterium glutamicum was genetically engineered to produce L-alanine from sugar under oxygen deprivation. The genes associated with production of organic acids in C. glutamicum were inactivated and the alanine dehydrogenase gene (alaD) from Lysinibacillus sphaericus was overexpressed to direct carbon
Senay Hamarat Baysal et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 35(4), 391-403 (2007-08-19)
Urease and AlaDH enzymes immobilized on active PEG derivatives were encapsulated at different ratios within sheep erythrocytes and their activity, encapsulation yields and erythrocyte recovery levels were assessed. Encapsulated derivatives were administered at given dosages and at given intervals to
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.

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