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L1006

Sigma-Aldrich

L-Lactic Dehydrogenase from bovine heart

Type XVII, buffered aqueous glycerol solution, ≥400 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

biological source

bovine heart

type

Type XVII

Assay

5.0—15.0 mg protein/mL (biuret)

form

buffered aqueous glycerol solution

specific activity

≥400 units/mg protein

mol wt

140 kDa

manufacturer/tradename

Sigma-Aldrich

technique(s)

cell based assay: suitable

impurities

<10 μg/mg protein free ammonium

color

white

pH

7.5

cation traces

NH4+: ≤10 μg/mg protein

UniProt accession no.

application(s)

life science and biopharma

foreign activity

glutamic-pyruvic transaminase and glutamic-oxalacetic transaminase ≤0.02%
pyruvate kinase, myokinase and α-glycerophosphate dehydrogenase ≤0.01%

storage temp.

2-8°C

Gene Information

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General description

Research area: Cell signaling. L-LacticDehydrogenase (LDH) is present in the cell cytoplasm. and is part of the glycolytic pathway. Lactate dehydrogenase (LDH) is a ubiquitous molecule found in plants, yeast, mammals, and microorganisms and is a member of the oxidoreductase family. It has five isozymes (LD1 to LD5) and this composition varies in different tissues. LD1 is present at higher concentrations in the heart, kidneys, and erythrocytes. LD5 is found in the liver and skeletal muscles.(2)

Application

L-Lactic Dehydrogenase from bovine heart has been used in ATPase assay of R2 complex Rvb1p-Rvb2p, RecA protein and sarcoplasmic reticulum Ca2+-ATPase (SERCA).

Biochem/physiol Actions

Variation in the levels of L-Lactic Dehydrogenase (LDH) isoform is a diagnostic marker for tissue damage. The levels of LDH is useful in detecting dairy cattle disease, Mastitis. Dye based purified LDH from bovine heart has analytical applications.Lactic dehydrogenase (LDH)plays an essential role in the glycolytic pathway where it is involved in the conversionof pyruvate to lactate using NAD+as a co-factor. It is considered an important molecule that can be used incancer therapy as it acts as a glycolytic inhibitor. Inhibition of LDH isassociated with blocking of aerobic glycolysis in the tumour cells.
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

Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5

Analysis Note

Protein determined by biuret

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1


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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Simultaneous purification of L-malate dehydrogenase and L-lactate dehydrogenase from bovine heart by biomimetic-dye affinity chromatography
Labrou NE and Clonis YD
Bioprocess and Biosystems Engineering, 16(3), 157-161 (1997)
Determination of lactate dehydrogenase (LDH) activity in milk by a fluorometric assay
Larsen T
The Journal of Dairy Research, 72(2), 209-216 (2005)
Monica Gallo et al.
Frontiers in bioscience (Landmark edition), 20(8), 1234-1249 (2015-05-12)
Despite the intense scientific efforts made, there are still many tumors that are difficult to treat and the percentage of patient survival in the long-term is still too low. Thus, new approaches to the treatment of cancer are needed. Cancer
Active displacement of RecA filaments by UvrD translocase activity
Petrova V, et al.
Nucleic Acids Research, 43(8), 4133-4149 (2015)
Purified E255L mutant SERCA1a and purified PfATP6 are sensitive to SERCA-type inhibitors but insensitive to artemisinins
Cardi D, et al.
The Journal of Biological Chemistry, 285(34), 26406-26416 (2010)

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