Pular para o conteúdo
Merck
Todas as fotos(1)

Documentos

73063

Sigma-Aldrich

Alanine Dehydrogenase, recombinant

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

Faça loginpara ver os preços organizacionais e de contrato


About This Item

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

recombinante

expressed in E. coli

forma

crystals
powder

atividade específica

≥15 U/mg

temperatura de armazenamento

−20°C

Aplicação

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 .

Ações bioquímicas/fisiológicas

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

Definição da unidade

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).

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

Resp. Sens. 1

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

Já possui este produto?

Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.

Visite a Biblioteca de Documentos

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
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
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.
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
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

Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.

Entre em contato com a assistência técnica