TargetMol

1-Oleoyl Lysophosphatidic Acid

Product Code:
 
TAR-T36907
Product Group:
 
Inhibitors and Activators
Supplier:
 
TargetMol
Regulatory Status:
 
RUO
Shipping:
 
cool pack
Storage:
 
-20℃
1 / 1
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CodeSizePrice
TAR-T36907-5mg5mg£153.00
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TAR-T36907-10mg10mg£218.00
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TAR-T36907-25mg25mg£398.00
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Further Information

Bioactivity:
1-Oleoyl lysophosphatidic acid is a species of lysophosphatidic acid (LPA) containing oleic acid at the sn-1 position. Phosphatidic acid is produced either directly through the action of phospholipase D (PLD) or through a two step process involving liberation of diacylglycerol (DAG) by phospholipase C (PLC) followed by phosphorylation of DAG by diglycerol kinase.[1] Hydrolysis of the fatty acid at the sn-2 position by phospholipase A2 (PLA2) yields bioactive LPA. LPA binds to one of five different G protein linked receptors to mediate a variety of biological responses including cell proliferation, smooth muscle contraction, platelet aggregation, neurite retraction, and cell motility.[2],[1] 1-Oleoyl lysophosphatidic acid is the most potent of the LPA analogs for calcium mobilization in A431 cells and for growth stimulation of a variety of cell lines.[3],[4]
CAS:
65528-98-5
Formula:
C21H41O7P
Molecular Weight:
436.5
Purity:
0.98
SMILES:
CCCCCCCC/C=CCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O

References

Noguchi, K., Ishii, S., and Shimizu, T. Identification of p2y9/GPR23 as a novel G protein-coupled receptor for lysophosphatidic acid, structurally distant from the Edg family. The Journal of Biological Chemisty 278(28), 25600-25606 (2003). Moolenaar, W.H. LPA: A novel lipid mediator with diverse biological actions. Trends in Cell Biology 4, 213-219 (1994). Jalink, K., Hengeveld, T., Mulder, S., et al. Lysophosphatidic acid-induced Ca2+ mobilization in human A4431 cells: Structure-activity analysis. Biochemistry Journal 307, 609-616 (1995). van Corven, E.J., van Rijswijk, A., Jalink, K., et al. Mitogenic action of lysophosphatidic acid and phosphatidic acid on fibroblasts. Dependence on acyl-chain length and inhibition by suramin. Biochemistry Journal 281, 163-169 (1992).