Rabbit anti Human Lyosphospholipid Phosphatase (LPP) 2
| Code | Size | Price |
|---|
| EXA-X1528P | 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. NOTE: Boiling LPP2 with sample buffer will aggregate the protein. Lysates should be prepared by mixing cells with lysis buffer (possibly with extra detergent) to solubilize the protein before adding sample buffer and lysate SHOULD NOT be boiled/heated.
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 2 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 2 protein.
Synonyms:
Lipid phosphate phosphohydrolase 2, EC 3.1.3.4, Phosphatidic acid, phosphatase 2c, PAP-2c, PAP2c, Phosphatidate phosphohydrolase type 2c, PAP2-gamma, PAP2-G
UniProt:
O43688 (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.