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L2625

Sigma-Aldrich

L-Lactic Dehydrogenase from bovine heart

Type III, ammonium sulfate suspension, ≥500 units/mg protein

Synonym(s):

Lactate, (S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type III

Quality Level

form

ammonium sulfate suspension

specific activity

≥500 units/mg protein

UniProt accession no.

foreign activity

pyruvate kinase ≤0.03%

storage temp.

2-8°C

Gene Information

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General description

Research area: Cell signaling

Lactate dehydrogenase (LDH) is a cytoplasmic enzyme that belongs to the oxidoreductase’s family. It is ubiquitously expressed in body tissues but at high levels in muscle, liver, and kidney. LDH exists as tetramer and comprises of two subunits (H and M). The LDH of eukaryotes undergo active-site loop gating for their catalytic functionality. L-lactate, which is the major enantiomeric form of lactate in vertebrates, is produced by the L-isomers of LDH enzyme encoded by the LDHC gene.

Application

L-Lactic Dehydrogenase from bovine heart has been used as a standard in cytotoxicity assay. It has also been used in glutamic pyruvic transaminase (GPT) assay.

Biochem/physiol Actions

Lactate dehydrogenase (LDH) is a crucial enzyme that plays a vital role in the anaerobic metabolic pathway. It facilitates the conversion of lactate to pyruvate and NAD⁺ to NADH, and vice versa, within cells. This enzymatic reaction plays a crucial role in cellular energy production, particularly in environments with low oxygen levels or hypoxic conditions. LDH activity is also significant in tumor glycolysis and the Warburg effect. LDH is released into the bloodstream when the cells are damaged or undergo death. Therefore, LDH can be used as a potential marker of cell injury and death. High lactate dehydrogenase activity is associated with various medical conditions, such as liver disease, anemia, heart attack, bone fractures, muscle trauma, and certain types of cancer.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

Unit Definition

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Physical form

Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0

Analysis Note

Protein determined by biuret

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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