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Key Documents

SAE0049

Sigma-Aldrich

Lactic Dehydrogenase, recombinant

from human, recombinant, expressed in E. coli, aqueous solution

Sinonimo/i:

(S)-Lactate: NAD+ oxidoreductase, L-Lactate Dehydrogenase

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero MDL:
Codice UNSPSC:
12352200
NACRES:
NA.54

Origine biologica

human

Livello qualitativo

Ricombinante

expressed in E. coli

Forma fisica

aqueous solution

Condizioni di stoccaggio

(Keep container tightly closed in a dry and well-ventilated place)

Colore

colorless

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... LDHA(3939)

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Descrizione generale

Research area: Cell Signaling
The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase.In particular, lactic dehydrogenase A (LDHA) is mainly found in skeletal muscle, and for that reason is known as the M subunit. This recombinant form of LDHA has a C-terminal histidine-tag.

Applicazioni

L-Lactate Dehydrogenase (LDHA) has been used in in vitro phosphoglycerate mutase 1 (PGAM1) inhibitors screening assay. It has also been used in a colorimetric assay for determining lactate concentration in conditioned media.

Azioni biochim/fisiol

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.  L-lactate dehydrogenase A chain (LDHA), an enzyme involved in pyruvate metabolism, LDH is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. LDHA regulates the microenvironment of developing tumors by the hypoxia-inducible factor (HIF)-signaling pathway. LDHA aids in the NAD+ regeneration during the β-oxidation of fatty acid. LDHA (L-lactate dehydrogenase A chain) is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. In cancer cells, HIF-1a (hypoxia-inducible factor) induces the expression of LDHA, which helps in maintaining glycolysis in cells.
L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.

Definizione di unità

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Stato fisico

Buffered aqueous solution with Hepes (pH 7.5), NaCl and glycerol.

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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LDHA is necessary for the tumorigenicity of esophageal squamous cell carcinoma.
Yao F, et al.
Tumour Biology : the Journal of the International Society For Oncodevelopmental Biology and Medicine, 34(1), 25-31 (2013)
Rapid and accurate determination of D- and L-lactate, lactose and galactose by enzymatic reactions coupled to formation of a fluorochromophore: Applications in food quality control
F. Shapiro, N. Silanikove
Food Chemistry, 119, 2-2 (2010)
Bovine CAPN1 maps to a region of BTA29 containing a quantitative trait locus for meat tenderness.
Smith T P L, et al.
Journal of Animal Science, 78(10), 2589-2594 (2000)
Effect of LDHA Inhibition on TNF-?-Induced Cell Migration in Esophageal Cancers
Forkasiewicz A, et al.
International Journal of Molecular Sciences, 23(24) (2022)
The Proteome of Human Liver Peroxisomes: Identification of Five New Peroxisomal Constituents by a Label-Free Quantitative Proteomics Survey
PLoS ONE, 8(2) (2013)

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