Cat No.
NATE-0982
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)
Alias
L-LDH; LAD; LD
Source
Porcine muscle
Species
Porcine
Bio-activity
>550 U/mg
Concentration
> 10 mg/mL
Appearance
White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5.
pH Stability
6.0-7.0
Stability
At +2 to +8°C within specification range for 12 months.
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).
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
