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840074P

Avanti

Soy PA

Avanti Research - A Croda Brand 840074P, powder

Synonyme(s) :

L-α-phosphatidic acid (Soy) (sodium salt)

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About This Item

Numéro CAS:
Code UNSPSC :
12352211
Nomenclature NACRES :
NA.25

Pureté

>99% (TLC)

Forme

powder

Conditionnement

pkg of 1 × 25 mg (840074P-25mg)

Fabricant/nom de marque

Avanti Research - A Croda Brand 840074P

Type de lipide

phosphoglycerides

Conditions d'expédition

dry ice

Température de stockage

−20°C

Chaîne SMILES 

[H][C@@](COP([O-])(O)=O)(OC(CCCCCCC/C=C\C/C=C\CCCCC)=O)COC(CCCCCCCCCCCCCCC)=O.[Na+]

Description générale

Phosphatidic acid (PA) is a diacyl-glycerophospholipid, with two fatty acids and a phosphate group that are covalently attached to a glycerol molecule through ester linkages. PA is synthesized by the activity of the endogenous enzyme phospholipase D or by supplementation with soy lecithin.

Application

Soy PA is suitable for use to study its effect on cell proliferation, nutrient sensing and to examine metabolic pathways in primary muscle cells of turbot (Scophthalmus maximus).

Actions biochimiques/physiologiques

Phosphatidic acid (PA) is a prime glycerophospholipid present in the biomembrane and is a precursor for phosphatidylcholine or phosphatidylserine. It has different functions in the cells like influencing the membrane curvature and signaling.

Conditionnement

5 mL Clear Glass Sealed Ampule (840074P-25mg)

Informations légales

Avanti Research is a trademark of Avanti Polar Lipids, LLC

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

No data available

Point d'éclair (°C)

No data available


Certificats d'analyse (COA)

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The mitotic and metabolic effects of phosphatidic acid in the primary muscle cells of turbot (Scophthalmus maximus)
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Joy JM, et al.
Nutrition, 11(1), 29-29 (2014)
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The Journal of biological chemistry, 288(32), 23090-23104 (2013-07-03)
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The Journal of biological chemistry, 290(23), 14289-14301 (2015-04-19)
Phosphatidylinositol (PI) 4,5-bisphosphate (PIP2) at the plasma membrane (PM) constitutively controls many cellular functions, and its hydrolysis via receptor stimulation governs cell signaling. The PI transfer protein Nir2 is essential for replenishing PM PIP2 following receptor-induced hydrolysis, but key mechanistic

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