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Merck

59747

Lactic Dehydrogenase, recombinant from E. coli

≥90 U/mg

Synonym(s):

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

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-617-8
MDL number:
EC Number:

Product Name

Lactic Dehydrogenase, recombinant from E. coli, ≥90 U/mg

recombinant

expressed in E. coli

form

powder

specific activity

≥90 U/mg

storage temp.

−20°C

Quality Level

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Application

Lactic Dehydrogenase, recombinant from E. coli has been used:
  • in lactate dehydrogenase (LDH) and malate dehydrogenase 1 (MDH1)assays and cross-linking assays
  • to prepare assay buffer to measure pyruvate kinase (PYK) by coupled assay
  • in in vitro DltC D-alanylation assay

Biochem/physiol Actions

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.
Conversion of L-lactate into L-pyruvate is crucial in hypoxic and anaerobic conditions, especially when synthesis of adenosine triphosphate (ATP) by oxidative phosphorylation is interrupted.

General description

LDH (lactic dehydrogenase), a glycolytic enzyme, particularly present in skeletal muscle, heart, liver, kidneys, brain, lungs and red blood cells. It has five isoenzyme forms. LDH possess a tetrameric structure.

Other Notes

One unit corresponds to the amount of enzyme which reduces 1 μmol pyruvate per minute at pH 7.4 and 25°C (NADH as cofactor)

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

ppe

Eyeshields, Gloves, type N95 (US)


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Circulating biomarkers in malignant melanoma
Advances in Clinical Chemistry, 69, 47-89 (2015)
An atypical glycolysis in Clostridium thermocellum
Zhou J, et al.
Applied and Environmental Microbiology, 39, AEM-04037 (2013)
Cardiac, Vascular, and Skeletal Muscle Systems
Haschek and Rousseaux's Handbook of Toxicologic Pathology (2013)
Lifeng Yang et al.
Med (New York, N.Y.), 3(2), 119-136 (2022-04-16)
Ketogenic diet is a potential means of augmenting cancer therapy. Here, we explore ketone body metabolism and its interplay with chemotherapy in pancreatic cancer. Metabolism and therapeutic responses of murine pancreatic cancer were studied using KPC primary tumors and tumor
A partial reconstitution implicates DltD in catalyzing lipoteichoic acid D-alanylation
Wood BM, et al.
The Journal of Biological Chemistry, 293(46), 17985-17996 (2018)

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