|Other Names||Aminopeptidase Q, AP-Q, 3411-, CHL2 antigen, Laeverin, AQPEP, LVRN|
|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||Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.|
|Cellular Location||Membrane; Single-pass type II membrane protein|
|Tissue Location||Specifically expressed in placenta and not in other tissues. Mainly found at the cell surface region of the extravillous trophoblasts. Detected on extravillous trophoblasts in the outer layer of the chorion laeve in the fetal membrane Not detected on either fetal amnionic epithelial cells or maternal decidual cells. Also detected in the migrating extravillous trophoblasts in the maternal decidual tissues (at protein level)|
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AQPEPis a metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.
Rose, J. Phd, et al. Mol. Med. (2010) In press :Maruyama, M., et al. J. Biol. Chem. 284(50):34692-34702(2009)Johnson, M.P., et al. Hum. Genet. 126(5):655-666(2009)Maruyama, M., et al. J. Biol. Chem. 282(28):20088-20096(2007)Haas, C.S., et al. Arthritis Rheum. 54(7):2047-2060(2006)
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