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SAE0049

Sigma-Aldrich

Lactic Dehydrogenase, recombinant

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

Synonyme(s) :

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

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.54

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli

Forme

aqueous solution

Conditions de stockage

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

Couleur

colorless

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

human ... LDHA(3939)

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Description générale

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.

Application

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.

Actions biochimiques/physiologiques

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+.

Définition de l'unité

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

Forme physique

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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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)
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)
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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