59747
Lactic Dehydrogenase, recombinant from E. coli
≥90 U/mg
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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
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)
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Med (New York, N.Y.), 3(2), 119-136 (2022-04-16)
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Wood BM, et al.
The Journal of Biological Chemistry, 293(46), 17985-17996 (2018)
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