The Autotaxin Sandwich ELISA is a quantitative immunoassay designed for in vitro measurement of ATX levels in cell culture supernatant or human and mouse biological fluids. Sample Volume: 5 µL Sample Number: 40 samples (in duplicate) / 96-well assay Sample Type: cell culture supernatant, sera, plasma, urine and ovarian ascites Species of Sample: mouse, human ATX
Product Background The ATX Sandwich ELISA provides a robust and simple method for researchers to measure ATX in biological samples. The concentration of ATX in the sample is determined using a standard curve of known amounts of ATX. Autotaxin, also known as ATX, ENPP2, lysophospholipase D (lysoPLD), phosphodiesterase 1alpha and plasma cell glycoprotein-1, is a secreted glycoprotein that is widely expressed with high levels in the serum. Via its lysoPLD activity, autotaxin hydrolyzes lysophosphatidylcholine (LPC) to generate the phospholipid growth factor lysophosphatidic acid (LPA). The enzymes same activity hydrolyzes sphingosylphosphorylcholine (SPC) to form sphinosine-1-phosphate (S1P). Autotaxin was first isolated as the autocrine motility factor secreted from melanoma cells. At that time, the enzymes lysoPLD activity had not been identified, so it was classified by homology to the ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) family of enzymes whose members hydrolyze phosphodiester bonds in various nucleotides and nucleotide derivatives. It was initially unclear how nucleotide hydrolysis could lead to the stimulation of cell motility. This mystery was solved when autotaxin was discovered to be identical to serum lysoPLD. Since then, the cancer-related activities of autotaxin, at least in cultured cells, have been attributed to the enzymes lysoPLD activity. In addition to cancer, autotaxin has been implicated in a number of diseases including obesity, arthritis, multiple sclerosis, Alzheimers disease and neuropathic pain. Featured in Publications 1. Benesch, M. G. K., et al. (2015). Regulation of autotaxin expression and secretion by lysophosphatidate and sphingosine-1-phosphate. Journal of Lipid Research 56: 1134-1144. 2. Bouchareb, R., et al. (2015). Autotaxin Derived From Lipoprotein(a) and Valve Interstitial Cells Promotes Inflammation and Mineralization of the Aortic Valve. Circulation 132: 677-690. 3. Black, K. E., et al. (2016). Autotaxin activity increases locally following lung injury, but is not required for pulmonary lysophosphatidic acid production or fibrosis. Faseb J 30: 2435-2450. 4. Nsaibia, M. J., et al. (2016). Autotaxin interacts with lipoprotein(a) and oxidized phospholipids in predicting the risk of calcific aortic valve stenosis in patients with coronary artery disease. Journal of Internal Medicine 280: 509-517. 5. Meng, G., et al. (2017). Implications for breast cancer treatment from increased autotaxin production in adipose tissue after radiotherapy. Faseb J 31: 4064-4077. 6. Lee, B.-H., et al. (2017). Effects of Gintonin-Enriched Fraction in an Atopic Dermatitis Animal Model: Involvement of Autotaxin Regulation. Biological and Pharmaceutical Bulletin 40(7): 1063-1070. 7. Nakamura, R., et al. (2017). Serum fatty acid-binding protein 4 (FABP4) concentration is associated with insulin resistance in peripheral tissues, A clinical study. PLoS ONE 12(6): e017973 |
