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Cat No.
NATE-1105
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, Recombinant (Porcine)
Alias
L-LDH
Species
Porcine
Form
In 3.2 M ammonium sulphate.
Enzyme Commission Number
EC 1.1.1.27
Bio-activity
335 U/mg protein at pH 7.0 and 37°C.
Molecular Mass
~ 36,000
pH Stability
6.0 - 10.0
Isoelectric point
~ 5.5
Unit Definition
One Unit of L-lactate dehydrogenase is defined as the amount of enzyme required to produce one μmole of NAD+ from NADH per minute.
Optimum pH
5.0 - 5.5
Optimum temperature
37°C
Thermal stability
up to 55°C
Stability
> 2 years at 4°C
Preparation Instructions
For assay, this enzyme should be diluted in Tris. HCl buffer (10 mM), pH 7.5 containing 1 mg/mL BSA. Swirl to mix the enzyme immediately prior to use.
Applications
High purity L-Lactate dehydrogenase (Porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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
