|Other Names||Group 3 secretory phospholipase A2, Group III secretory phospholipase A2, GIII sPLA2, sPLA2-III, Phosphatidylcholine 2-acylhydrolase 3, PLA2G3|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage: 1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE. Plays a role in ciliogenesis.|
|Cellular Location||Secreted. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole|
|Tissue Location||Expressed in kidney, heart, liver, and skeletal muscle. Also present in placenta and peripheral blood leukocytes. Not detected in brain, colon, thymus, spleen and small intestine. In lung, expressed in bronchial epithelial cells and alveolar macrophages, but scarcely detected in alveolar epithelium, arterial walls and interstitial fibroblasts (at protein level). In joints of osteoarthritis and rheumatoid arthritis, expressed in endothelial cells (at protein level). In normal heart, detected in some vessels. In myocardial tissues with acute infarction, expressed in vascular endothelial cells adjacent to cardiomyocytes and those in lesions with granulation Expression in cardiomyocytes is scarce (at protein level). In uterus, breast and colon cancers, detected in tumor cells and neighboring microvascular endothelium, but not in normal glandular tissues (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
PLA2G3 belongs to the family of secreted phospholipase A2(sPLA2; EC 188.8.131.52) proteins. These Ca(2+)-dependent lipolyticenzymes have a conserved Ca(2+)-binding loop and a his-asp dyad inthe catalytic site (Murakami et al., 2003 [PubMed12522102]).
Wang, G., et al. J. Neurochem. 114(4):1039-1048(2010)Yoshida, T., et al. Int. J. Mol. Med. 25(4):649-656(2010)Segat, L., et al. Vaccine 28(10):2201-2206(2010)Oguri, M., et al. Am. J. Hypertens. 23(1):70-77(2010)Sato, H., et al. Biochem. J. 421(1):17-27(2009)
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