|Application ||WB, IHC-P, FC, E|
|Calculated MW||58304 Da|
|Antigen Region||409-438 aa|
|Other Names||Fatty-acid amide hydrolase 2, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2, AMDD|
|Target/Specificity||This FAAH2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 409-438 amino acids from the C-terminal region of human FAAH2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||FAAH2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.|
|Cellular Location||Membrane; Single-pass membrane protein|
|Tissue Location||Highly expressed in the brain, small intestine and testis. Also expressed in the heart, kidney, liver, lung and prostate.|
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Provided below are standard protocols that you may find useful for product applications.
FAAH2 encodes a fatty acid amide hydrolase that shares a conserved protein motif with the amidase signature family of enzymes. The encoded enzyme is able to catalyze the hydrolysis of a broad range of bioactive lipids, including those from the three main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. This enzyme has a preference for monounsaturated acyl chains as a substrate.
Kaczocha, M., et al. J. Biol. Chem. 285(4):2796-2806(2010)
Karbarz, M.J., et al. Anesth. Analg. 108(1):316-329(2009)
Wei, B.Q., et al. J. Biol. Chem. 281(48):36569-36578(2006)
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