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Native Lactate Dehydrogenase from Thermophillic bacteria

Cat No.
DIA-400
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, Native (Thermophillic bacteria)
Alias
LDH
Source
Thermophillic bacteria
Applications
Diagnostic test and biosensors; NADH recycling. This enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing.
Form
Frozen Liquid
Enzyme Commission Number
EC 1.1.1.27
CAS No.
9001-60-9
Unit Definition
One unit is defined as the amount of enzyme oxidizing 1μmol of NADH per 1 minute (ε340 = 6.22 mM-1 cm-1).
Optimum pH
~8.0
Optimum temperature
70°C
Thermal stability
~100% stability after 1 hour at 70°C
Storage
Store at -20°C
Buffer
20 mM Tris-HCl (pH 8.0)
Synonyms
Lactate dehydrogenase; EC 1.1.1.27; LDH; LD

"LDH" Total Products Page

Catalog Product Name EC No. CAS No. Source Price
NATE-1793 L-Lactate Dehydrogenase (Crude Enzyme) EC 1.1.1.27 9001-60-9 E. coli Inquiry
NATE-1681 Native Human Lactate Dehydrogenase EC 1.1.1.27 9001-60-9 Human Muscle Inquiry
NATE-1680 Native Human Lactate Dehydrogenase EC 1.1.1.27 9001-60-9 Human Heart Inquiry
NATE-1105 L-Lactate Dehydrogenase from Porcine, Recombinant EC 1.1.1.27 9001-60-9 Porcine Inquiry
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