Passa al contenuto
Merck
Tutte le immagini(1)

Documenti

LMDH-RO

Roche

L-Malate Dehydrogenase (L-MDH)

from pig heart (mitochondrial)

Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali


About This Item

Classificazione EC (Enzyme Commission):
Codice UNSPSC:
12352202

Origine biologica

Porcine heart (mitochondrial)

Livello qualitativo

Forma fisica

solution
suspension

Attività specifica

~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.)

Confezionamento

pkg of 1 mL (10127248001 solution)
pkg of 1 mL (10127256001 suspension)
pkg of 5 mL (10127914001suspension)

Produttore/marchio commerciale

Roche

tecniche

activity assay: suitable

Colore

white

pH ottimale

7.4-7.5(reduction of oxaloacetate)
9.2-9.5(oxidation of malate)

Solubilità

water: miscible

Compatibilità

suitable for Western blot

N° accesso NCBI

N° accesso UniProt

applicazioni

life science and biopharma

Attività estranea

Fumarase <0.01%
GIDH 0.001%
GOT 0.001%
GPT 0.00185%
LDH <0.01%
NADH oxidase <0.001%

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

Informazioni sul gene

Porcine ... MDH2(397039)

Descrizione generale

L-malate:NAD+ oxidoreductase
The L-malate dehydrogenase enzyme is a nuclear gene product that is synthesized with a 24-residue amino-terminal signal peptide. This peptide is proteolytically cleaved during the translocation of the enzyme to the mitochondrial matrix.

Applicazioni

The enzyme L-malate dehydrogenase from pig heart has been used to measure PEPCK (phosphoenolpyruvate carboxykinase) activity. The oxaloacetate, produced by PEPCK, is reduced to malate via the oxidation of NADH, which in turn is measured at 340 nm using a spectrophotometer. The enzyme has also been used to measure oxaloacetate by measuring the reduction in NADH spectroscopically at 340 nm.

Azioni biochim/fisiol

The enzyme L-malate dehydrogenase from pig heart catalyzes the oxidation of L-malate to oxaloacetate. The enzyme is an NAD-dependent mitochondrial dehydrogenase that functions in the tricarboxylic acid cycle. It is a component of the malate-aspartate shuttle that transports reducing equivalents across the inner mitochondrial membrane in the form of malate.

Qualità

Contaminants: <0.002% GOT, <0.01% fumarase and LDH, each luM each, <0.02% HK, <0.002% PGI

Stato fisico

Solution in 50% glycerol (v/v), pH approximately 7
Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

Nota sulla preparazione

Activator: – phosphate
– arsenate
– Mg2+
– Zn2+

Altre note

For life science research only. Not for use in diagnostic procedures.

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

No data available

Punto d’infiammabilità (°C)

No data available


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

Possiedi già questo prodotto?

I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

Visita l’Archivio dei documenti

Extraction and Measurement the Activities of Cytosolic Phosphoenolpyruvate Carboxykinase (PEPCK) and Plastidic NADP-dependent Malic Enzyme (ME) on Tomato (Solanum lycopersicum).
Osorio, S et al.
Bio-protocol, 4 (2014)
Agata M Pudlik et al.
Journal of bacteriology, 193(3), 706-714 (2010-12-01)
Carbohydrate/citrate cometabolism in Lactococcus lactis results in the formation of the flavor compound acetoin. Resting cells of strain IL1403(pFL3) rapidly consumed citrate while producing acetoin when substoichiometric concentrations of glucose or l-lactate were present. A proton motive force was generated
S L Roderick et al.
The Journal of biological chemistry, 261(20), 9461-9464 (1986-07-15)
In a previous study, we reported the apparent similarity between a low resolution electron density map of mitochondrial malate dehydrogenase and a model of cytoplasmic malate dehydrogenase (Roderick, S. L., and Banaszak, L. J. (1983) J. Biol. Chem. 258, 11636-11642).

Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..

Contatta l'Assistenza Tecnica.