Rabbit anti Human Lyosphospholipid Phosphatase (LPP) 3
| Code | Size | Price |
|---|
| EXA-X1529P | 100 ug | £316.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Rabbit
Antibody Isotype: IgG
Antibody Clonality: Polyclonal
Regulatory Status: RUO
Target Species: Human
Shipping:
Ship at ambient temperature freeze upon arrival
Storage:
Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles
Further Information
Applications Description:
This antibody can be used for Western blotting (10-15 ?g/ml). Optimal concentration should be evaluated by serial dilutions.
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].
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.
Concentration:
See vial for concentration
Field of Interest:
Signal Transduction
Formulation:
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Functional Analysis:
Western Blotting
Immunogen:
Unique peptide derived from the human lysophospholipid phosphatase 3 protein.
Positive Control:
Transfected HEK-293 cells
Product:
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Product Form:
Unconjugated
Product Stability:
Products are stable for one year from purchase when stored properly
Purification Method:
Ammonium Sulfate Precipitation
Source:
Rabbits were immunized with a unique peptide derived from the human lysophospholipid phosphatase 3 protein.
Synonyms:
Lipid phosphate phosphohydrolase 3, EC 3.1.3.4 Phosphatidic acid phosphatase 2b, PAP2-beta ,PAP-2b, PAP2b, Phosphatidate phosphohydrolase type 2b, Vascular endothelial growth factor and type I collagen-inducible protein, VCIP
UniProt:
O14495 (Human)
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, 24281-24284.
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.
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, 24281-24284.
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.