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Merck

SAE0049

Sigma-Aldrich

Lactic Dehydrogenase, recombinant

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

Sinónimos:

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

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352200
NACRES:
NA.54

origen biológico

human

Nivel de calidad

recombinante

expressed in E. coli

Formulario

aqueous solution

condiciones de almacenamiento

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

color

colorless

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

Información sobre el gen

human ... LDHA(3939)

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Descripción general

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.

Aplicación

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.

Acciones bioquímicas o fisiológicas

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+.

Definición de unidad

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

Forma física

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

Producto relacionado

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Comparative transcriptome analysis reveals the potential influencing mechanism of dietary astaxanthin on growth and metabolism in Litopenaeus vannamei
Yichao W, et al.
Aquaculture Research (2020)
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)
LDH-A regulates the tumor microenvironment via HIF-signaling and modulates the immune response
Serganova I, et al.
PLoS ONE, 13(9) (2018)
Effect of LDHA Inhibition on TNF-?-Induced Cell Migration in Esophageal Cancers
Forkasiewicz A, et al.
International Journal of Molecular Sciences, 23(24) (2022)

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