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Antibody detects endogenous levels of total PLA1A.
PLA1A is a phospholipase that hydrolyzes fatty acids at the sn-1 position of phosphatidylserine and 1-acyl-2-lysophosphatidylserine. This secreted protein hydrolyzes phosphatidylserine (PS) in liposomes and can also hydrolyze PS in apoptotic cells and activate platelets where the resulting 2-acyl-lysophosphatidylserine acts as a lipid mediator for mast cells, T cells, and neural cells, suggesting that a major function of PLA1A may be the production of lysophospholipid mediators. PLA1A is upregulated in rat peripheral blood cells bearing long-term surviving cardiac allograft. PLA1A is also expressed in human THP-1-derived macrophages and this expression is upregulated in cells treated with lipopolysaccharide, a TLR4 ligand. This upregulation is inhibited with corticosteroids, which are often used at high dosages to suppress chronic allograft rejection.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Phosphatidylserine-specific phospholipase A1; phosphatidylserine-specific phospholipase A1alpha; Phospholipase A1 member A; PS-PLA1
Gene Aliases: AA986889; NMD; PLA1A; PS-PLA1; PSPLA1
UniProt ID: (Human) Q53H76, (Rat) P97535, (Mouse) Q8VI78
Entrez Gene ID: (Human) 51365, (Rat) 85311, (Mouse) 85031
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