59747
Lactic Dehydrogenase, recombinant
≥90 U/mg
Sinónimos:
(S)-Lactate: NAD+ oxidoreductase, L-Lactate Dehydrogenase
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About This Item
Productos recomendados
recombinant
expressed in E. coli
Quality Level
form
powder
specific activity
≥90 U/mg
storage temp.
−20°C
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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.
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.
Unit Definition
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)
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
ppe
Eyeshields, Gloves, type N95 (US)
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