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L-Lactic Dehydrogenase from Bacillus stearothermophilus, Recombinant

Cat No.
NATE-0382
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
LDH, Recombinant (Bacillus stearothermophilus)
Alias
LDH; LD
Source
E. coli
Species
Bacillus stearothermophilus
Product Overview
recombinant, expressed in E. coli, lyophilized powder, > 200 units/mg protein (Lowry)
Form
lyophilized powder
Enzyme Commission Number
EC 1.1.1.27
Activity
> 200 units/mg protein (Lowry)
CAS No.
9001-60-9
Unit Definition
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 6.0 at 30°C.
Stability
2-8°C
Stabilizers
Lyophilized powder containing triethanolamine, buffer salts, EDTA and stabilizer
Buffer
Lyophilized powder containing triethanolamine, buffer salts, EDTA and stabilizer
Synonyms
EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase
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Related Services
Related Protocols
L-LACTIC DEHYDROGENASE -Enzymatic Assay Protocol
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