|Other Names||Abhydrolase domain-containing protein 2, 311-, Lung alpha/beta hydrolase 2, Protein PHPS1-2, ABHD2, LABH2|
|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||Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane (PubMed:26989199). Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA) (PubMed:26989199). Plays a key role in sperm capacitation in response to progesterone by mediating degradation of 2AG, an inhibitor of the sperm calcium channel CatSper, leading to calcium influx via CatSper and sperm activation (PubMed:26989199). May also play a role in smooth muscle cells migration (By similarity).|
|Cellular Location||Cell projection, cilium, flagellum membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein|
|Tissue Location||Present in sperm (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a protein containing an alpha/betahydrolase fold, which is a catalytic domain found in a very widerange of enzymes. The function of this protein has not beendetermined. Alternative splicing of this gene results in twotranscript variants encoding the same protein. [provided byRefSeq].
Giambra, V., et al. J. Immunol. 183(12):8280-8285(2009)Miyata, K., et al. Biochem. Biophys. Res. Commun. 365(2):207-213(2008)Edgar, A.J., et al. Biochem. Biophys. Res. Commun. 292(3):617-625(2002)Rapiejko, P.J., et al. Nucleic Acids Res. 16 (17), 8721 (1988) :
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