Cat No.
NATE-0413
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 (Rabbit)
Alias
L-LDH; LAD; LD
Source
Rabbit muscle
Species
Rabbit
Form
Type I, lyophilized powder; Type II, ; Type III, ammonium sulfate suspension, Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0.
Enzyme Commission Number
EC 1.1.1.27
Bio-activity
>90%. (>200U/mL)
CAS No.
9001-60-9
Isoelectric point
8.4-8.6
Unit Definition
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37°C.
Optimum pH
7.5
Warnings
Protein determined by biuret.
Synonyms
EC 1.1.1.27; 9001-60-9; 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