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10107085001

Roche

L-Lactate Dehydrogenase (L-LDH)

from hog muscle

Synonym(s):

L-LDH, L-Lactate Dehydrogenase, L-lactate

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204

biological source

hog muscle

Quality Level

form

suspension

specific activity

~550 units/mg protein (at 25 °C (1,000 U/mg at 37 °C) with pyruvate as the substrate.)

packaging

pkg of 10 mL (100 mg)

manufacturer/tradename

Roche

Related Categories

General description

L-Lactate Dehydrogenase (L-LDH) is an enzyme which is involved in the glycolytic pathway. It is believed to consist of five isotypes, LDH1 to LDH5. It also has a major role in carbohydrate metabolism of human malaria parasites.

Application

It was used in determination of D-Lactate.
Reduction of α-ketoacids to α-hydroxycarboxylic acids or reverse reaction.

Physical form

Suspension in 3.2 M ammonium sulfate solution, pH approximately 6.5

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Thorsten Irsch et al.
The Journal of biological chemistry, 279(21), 22209-22217 (2004-02-21)
The glyoxalase system is a ubiquitous pathway catalyzing the glutathione-dependent detoxication of ketoaldehydes such as methylglyoxal, which is mainly formed as a by-product of glycolysis. The gene encoding a glyoxalase II has been cloned from Trypanosoma brucei, the causative agent
Plasmodium falciparum and Plasmodium vivax: Lactate-Dehydrogenase Activity and Its Application for in Vitro Drug Susceptibility Assay.
Basco, Leonardo K., et al.
Experimental Parasitology, 80.2, 260-271 (1995)
Mizeck Gg Chagunda et al.
The Journal of dairy research, 73(4), 431-440 (2006-07-11)
Systematic factors affecting the activities of L-lactate dehydrogenase (LDH) and N-acetyl-beta-D-glucosaminidase (NAGase) and somatic cell count (SCC), the association between the activities of LDH and NAGase and SCC with respect to udder health status, and the ability of LDH and
Heiko Henning et al.
Andrology, 10(7), 1426-1440 (2022-07-06)
Prolonging the shelf-life of liquid-preserved semen without compromising its fertilizing capacity may increase the efficiency of artificial insemination in pigs. Many fertilization-relevant processes are adenosine triphosphate dependent. The impact of semen storage and rewarming to body temperature on the energy

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