Description
A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.
Abbr
L-LDH, Native (Porcine)
Applications
Use L-Lactate Dehydrogenase in a variety of diagnostic tests for the removal of pyruvate in determinations working with NADH (i.e., triglycerides, lipase, aldolase, aminotransferases, glutamate dehydrogenase).
Appearance
White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5.
Product Overview
Dehydrogenase that catalyzes the interconversion of specific for L(+)-lactate to pyruvate. Apply this ready-to-use enzyme directly in your diagnostic test. Rely on the proven diagnostic quality of this product.
Contaminants
Aldolase: <0.001 Glutamate dehydrogenase: <0.01 Aspartate aminotransferase (AST/GOT): <0.005 Alanine aminotransferase (ALT/GPT): <0.005 Malate dehydrogenase: <0.01 Myokinase: <0.01 Pyruvate kinase: <0.001
Stability
At +2 to +8°C within specification range for 12 months.
Synonyms
lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate
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