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ENPP2 / Autotaxin Antibody (aa698-712)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q13822 |
| Reactivity | Human, Monkey |
| Host | Goat |
| Clonality | Polyclonal |
| Calculated MW | 99kDa |
| Dilution | ELISA (1:128000), IHC-P (5 µg/ml), WB (0.3-1 µg/ml) |
| Gene ID | 5168 |
|---|---|
| Other Names | Ectonucleotide pyrophosphatase/phosphodiesterase family member 2, E-NPP 2, 3.1.4.39, Autotaxin, Extracellular lysophospholipase D, LysoPLD, ENPP2, ATX, PDNP2 |
| Target/Specificity | Human ENPP2 / Autotaxin. This antibody is expected to recognize all reported isoforms (NP_006200.3; NP_001035181.1, NP_001124335.1). |
| Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
| Precautions | ENPP2 / Autotaxin Antibody (aa698-712) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ENPP2 (HGNC:3357) |
|---|---|
| Function | Secreted lysophospholipase D that hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:12354767, PubMed:14500380, PubMed:15769751, PubMed:26371182, PubMed:27754931). Its major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:14500380, PubMed:27754931). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed:14500380). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:12176993, PubMed:15769751). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation (PubMed:11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin- sensitive G protein (PubMed:1733949). May have a role in induction of parturition (PubMed:12176993). Possible involvement in cell proliferation and adipose tissue development (Probable). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (PubMed:21393252). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3- phosphocholine (lyso-PAF) (PubMed:21393252). |
| Cellular Location | Secreted |
| Tissue Location | Detected in blood plasma (at protein level) (PubMed:12176993, PubMed:26371182). Predominantly expressed in brain, placenta, ovary, and small intestine. Expressed in a number of carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma and non-small-cell lung cancer. Expressed in body fluids such as plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic fluids. Not detected in leukocytes. Isoform 1 is more highly expressed in peripheral tissues than in the central nervous system (CNS) Adipocytes only express isoform 1. Isoform 3 is more highly expressed in the brain than in peripheral tissues. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility- related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor.
References
Murata J.,et al.J. Biol. Chem. 269:30479-30484(1994).
Kawagoe H.,et al.Genomics 30:380-384(1995).
Lee H.Y.,et al.Biochem. Biophys. Res. Commun. 218:714-719(1996).
van Meeteren L.A.,et al.J. Biol. Chem. 280:21155-21161(2005).
Giganti A.,et al.J. Biol. Chem. 283:7776-7789(2008).
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