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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
Download
Download Datasheet| 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 |