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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:
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.54

biological source

human

Quality Level

recombinant

expressed in E. coli

form

aqueous solution

storage condition

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

color

colorless

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... LDHA(3939)

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General description

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.

Biochem/physiol Actions

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+.

Unit Definition

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

Physical form

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Visite la Librería de documentos

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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