Recombinant Human FAAH2 protein is a Human Full Length protein, in the 1 to 532 aa range, expressed in Wheat germ and suitable for ELISA, WB.
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
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Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:17015445, PubMed:19926788). Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.
AMDD, FAAH2, Fatty-acid amide hydrolase 2, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2
Recombinant Human FAAH2 protein is a Human Full Length protein, in the 1 to 532 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:17015445, PubMed:19926788). Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.
Belongs to the amidase family.
FAAH2 (Fatty Acid Amide Hydrolase 2) is an enzyme that breaks down fatty acid amides. FAAH2 shows structural similarity to FAAH but has distinct substrate specificity. The approximate molecular mass of FAAH2 is 63 kDa. It is widely expressed in several human tissues including the brain liver and kidneys among others. Understanding FAAH2's mechanical role can offer insights into its biological functions and applications in research.
FAAH2 acts in regulating lipid signaling pathways by hydrolyzing bioactive fatty acid amides. Unlike FAAH FAAH2 appears less efficient in degrading some endocannabinoids suggesting a unique role in signaling processes. It does not function as part of a larger protein complex but its activity results in bioactive lipids important for various cellular responses. This regulation helps maintain cellular lipid balance and influences cellular communication.
FAAH2 participates in the endocannabinoid and lipid signaling pathways. It helps modulate local levels of fatty acid amides affecting synaptic plasticity and pain perception. FAAH2 is related to proteins like FAAH through shared involvement in these pathways which manage neurotransmitter release and reception. Understanding FAAH2's placement and function within these pathways can help in designing new therapeutic approaches.
FAAH2 shows potential links to neurological conditions and metabolic disorders. Altered FAAH2 activity may contribute to mood disorders due to its role in endocannabinoid regulation. FAAH2 also has a potential relationship with obesity where altered lipid signaling disrupts energy balance. FAAH closely associated with FAAH2 might share overlapping physiological roles that could influence disease outcomes when FAAH2 function is disrupted. Research into the links of FAAH2 with disorders provides avenues for targeted therapies.
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ab165703 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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