59747

Lactic Dehydrogenase, recombinant

≥90 U/mg

• Synonyme(s) : (S)-Lactate: NAD⁺ oxidoreductase, L-Lactate Dehydrogenase
• Numéro CAS: 9001-60-9
• UNSPSC Code: 12352204
• NACRES: NA.54
• EC Number: 232-617-8
• MDL number: MFCD00131466
• Numéro CE : 1.1.1.27 (BRENDA, IUBMB)
• Specific activity: ≥90 U/mg
• Recombinant: expressed in E. coli

Propriétés

• recombinant: expressed in E. coli
• Quality Segment: 100
• form: powder
• specific activity: ≥90 U/mg
• storage temp.: −20°C

Description

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.

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)

Informations sur la sécurité

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• pcodes: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Classe de stockage: 11 - Combustible Solids
• wgk: WGK 1
• ppe: Eyeshields, Gloves, type N95 (US)