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FAAH2 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q6GMR7 |
|---|
| Gene ID | 158584 |
|---|---|
| Other Names | Fatty-acid amide hydrolase 2, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2, AMDD |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | FAAH2 |
|---|---|
| Synonyms | AMDD |
| Function | 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. |
| Cellular Location | Membrane; Single- pass membrane protein. Lipid droplet |
| Tissue Location | Expressed in kidney, liver, lung, prostate, heart and ovary. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
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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