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
recombinant
expressed in E. coli
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
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.
L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.
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)
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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