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8,11,14-Eicosatriynoic Acid (Synonyms: 8,11,14-ETI)

Catalog No.GC15338

A Cox, 12-LO, and 5-LO inhibitor

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8,11,14-Eicosatriynoic Acid Chemical Structure

Cas No.: 34262-64-1

Taille Prix Stock Qté
1mg
170,00 $US
En stock
5mg
596,00 $US
En stock

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Sample solution is provided at 25 µL, 10mM.

Description Chemical Properties Product Documents Related Products

8,11,14-Eicosatriynoic Acid, as an inhibitor of prostaglandin, leukotriene biosynthesis, and arachidonic acid induced platelet aggregation, blocks human 12-lipoxygenase (12-LO), cyclooxygenase (COX), and 5-lipoxygenase (5-LO) with IC50 values of 0.46 μM, 14 μM, and 25 μM, respectively. Also, it inhibits the actions of slow-reacting substance of anaphylaxis with an IC50 value of 10 μM [1,2].

Lipoxygenases are found widely in fungi, plants, and animals in high levels. 12-LO is involved in a number of significant disease states and may play a role in oxidative glutamate toxicity. COX enzymes play elaborate roles in human physiology and pathology, involving neuronal, immune, renal, cardiovascular, gastrointestinal, and reproductive systems. COX enzymes are blocked by aspirin and a wide variety of other non-steroidal anti-inflammatory drugs, which makes them important clinically [3]. 5-LO is involved in cancer pathobiology. It is expressed by a variety of cancer cells including colon, lung, breast, and prostate and promotes cancer cell growth and neo-angiogenesis.

In vitro: Up to now, in vitro study of 8,11,14-Eicosatriynoic Acid is still in the development stage.

In vivo: Up to now, in vivo study of 8,11,14-Eicosatriynoic Acid is still in the development stage.

References:
[1].  Goetz, J., Sprecher, H., Cornwell, D., & Panganamala, R. Inhibition of prostaglandin biosynthesis by triynoic acids. Prostaglandins. 1976; 12(2): 187-192.
[2].  Sun, F., McGuire, J., Morton, D., Pike, J., Sprecher, H., & Kunau, W. Inhibition of platelet arachidonic acid 12-lipoxygenase by acetylenic acid compounds. Prostaglandins. 1981; 21(2): 333-343.
[3].  Fitzpatrick, F. Cyclooxygenase Enzymes: Regulation and Function. Current Pharmaceutical Design. 2004; 10(6): 577-588.

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