Lactate Dehydrogenase (LDH)

Catalogue Number: 350-80
Product Name Lactate Dehydrogenase
Source Porcine Heart
Catalogue Number 350-80
Purity Purified
Form Liquid
Activity > 5,000 U/mL (Dimension® Clinical Chemistry System)
Unit Definition One unit will catalyze the oxidation of one micromole of L-lactate to pyruvate with simultaneous reduction of NAD+ to NADH per minute at 37°C and pH 9.4.
Protein > 15 mg/mL (Coomassie)
Specific Activity > 200 U/mg protein
Contaminants AST/SGOT: < 0.1%
ALT/SGPT: < 0.06%
MDH: < 0.06%
PK: < 0.06%
Appearance Cloudy, white suspension
Formulation Suspension in 2.5 M ammonium sulfate with 0.1 M sodium phosphate, pH 7.0.
Recertification 2 years
Storage 2-8°C
Reaction Catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back.
Synonyms LDH, Lactic Dehydrogenase
Molecular Weight ~136,700 (Huston et al. 1972)
CAS Number 9001-60-9
E.C. Number

Lee Biosolutions produces Porcine Heart Lactate Dehydrogenase (LDH) for medical research and diagnostic manufacturing uses.

Custom preparations, technical support, bulk quantities and aliquoting available, email for more details.

Lactate dehydrogenase (LDH) is an enzyme (EC present in a wide variety of organisms, including plants and animals. Lactate Dehydrogenase catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LD can also catalyze the oxidation of hydroxybutyrate, Lactate Dehydrogenase (LDH) is occasionally called Hydroxybutyrate Dehydrogenase (HBD).

Lactate Dehydrogenase enzyme is also found in cerebrospinal fluid where high levels of lactate dehydrogenase in cerebrospinal fluid are often associated with bacterial meningitis. High levels of Lactate Dehydrogenase (LDH) enzyme can also be found in cases of viral meningitis, generally indicating the presence of encephalitis and poor prognosis.

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