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SAE0049 Sigma-Aldrich

L-Lactate Dehydrogenase (LDHA)

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

Synonym: (S)-Lactate: NAD+ oxidoreductase, L-Lactate Dehydrogenase, Lactate, Lactic Dehydrogenase, recombinant from E. coli

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Properties

biological source   human
recombinant   expressed in E. coli
form   aqueous solution
shipped in   dry ice
storage temp.   −20°C

Description

Biochem/physiol Actions

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.<REFERENCE ID="99180" TYPE="literature"/>
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.

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.

General description

L-lactate dehydrogenase (LDH) is an enzyme that catalyzes the conversion of lactate to pyruvate. 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.
The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
Protocols & Articles
Peer-Reviewed Papers
15

References

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