Background: Phosphatidic acid phosphatase type 2 (PAP2) was originally identified as a plasma membrane enzyme that catalyses the dephosphorylation of the putative second messenger, phosphatidic acid (PA) to diacylglycerol (DG) [1]. Subsequently, multiple isoforms of PAP2 were cloned [2-5]. It was found that these enzymes dephosphorylate a number of lipid phosphates in vitro other than PA, including the potent bioactive lipids, lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P). Therefore, they have been renamed lipid phosphate phosphatases (LPPs). Currently, there are four members of this family called LPP1, LPP1a, LPP2 and LPP3 [6]. S1P [7] and LPA [8] regulate the proliferation, differentiation, apoptosis and migration of cells by binding to a family of G protein-coupled receptors. Thus, EDG1/S1P1, EDG3/S1P3, EDG5/S1P2/AGR16/H218, EDG6/S1P4 and EDG8/S1P5/nrg-1 are high affinity S1P receptors [7] whereas EDG2/LPA1, EDG4/LPA2 and EDG7/LPA3 have high affinity for LPA [8]. Recently, the over-expression of LPP1 was shown to limit LPA-stimulated signalling in Rat2 fibroblasts [9] and LPA-stimulated DNA synthesis in HEK 293 cells [10]. Similarly, over-expression of LPP1, LPP1a and LPP2 attenuate S1P-signalling to the p42/p44 mitogen activated protein kinase cascade [11].
Positive Control: Transfected HEK-293 cells
Purification Method: Ammonium Sulfate Precipitation
Concentration: See vial for concentration
Source: Rabbits were immunized with a unique peptide derived from the human lysophospholipid phosphatase 3 protein.
References: 1. Jamal, Z., et al. (1991) Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol. J. Biol. Chem. 266, 2988-2996.2. Kai, M., et al. (1997) Cloning and characterisation of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J. Biol. Chem. 272, 24572-24578.3. Roberts, R., et al. (1998) Human type 2 phosphatidic phosphohydrolases. Substrate specificity of the type 2a, 2b and 2c enzymes and cell surface activity of the 2a isoforms. J. Biol. Chem. 273, 22059-22067.4. Leung, D.W., et al. (1998) Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell. Biol. 17, 377-385.5. Tate, R.J., et al. (1999) Molecular cloning of magnesium-independent type 2 phosphatidic acid phosphatases from airway smooth muscle. Cell. Signal. 11, 515-522.6. Brindley, D.N & Waggoner, D.W. (1998) Mammalian lipid phosphate phosphohydrolases. J. Biol. Chem. 273, 24281-2428.7. Pyne, S. & Pyne, N.J. (2000) Sphingosine 1-phosphate in mammalian cells. Biochem. J. 349, 385-402.8. Kranenberg, O. & Moolenaar, W.H. (2001) Ras-MAP kinase signaling by lysophosphatidic acid and other G protein-coupled receptor agonists. Oncogene 20 1540-1546.9. Xu, J., et al. (2000) Lipid phosphate phosphatase-1 and Ca2+ control lysophosphatidate through EDG-2 receptors. J. Biol. Chem. 275, 27520-27530.10. Hooks, S.B., et al. (2001) Lysophosphatidic acid induced mitogenesis is regulated by lipid phosphate phosphatases and is EDG receptor independent. J. Biol. Chem. 276, 4611-4621.11. Alderton, F., et al. (2001) J. Biol. Chem. 276, 13452-13460.
UniProt: O14495 (Human)
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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