| Reaction Details |
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 | Report a problem with these data |
| Target | Fatty acid-binding protein 5-ANS |
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| Ligand | BDBM22988 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | Fluorescence Competition Assay |
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| Kd | 100.3±8.3 nM |
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| Citation |  Yu, S; Levi, L; Casadesus, G; Kunos, G; Noy, N Fatty acid-binding protein 5 (FABP5) regulates cognitive function both by decreasing anandamide levels and by activating the nuclear receptor peroxisome proliferator-activated receptor ß/d (PPARß/d) in the brain. J Biol Chem289:12748-58 (2014) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Fatty acid-binding protein 5-ANS |
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| Name: | Fatty acid-binding protein 5-ANS |
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| Synonyms: | FABP5-ANS |
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| Type: | Protein |
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| Mol. Mass.: | n/a |
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| Description: | n/a |
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| Components: | This complex has 2 components. |
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| Component 1 |
| Name: | Fatty acid-binding protein 5 |
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| Synonyms: | FABP5_MOUSE | Fabp5 | Fabpe | Fatty acid-binding protein 5 (FABP5) | Klbp | Mal1 |
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| Type: | Protein |
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| Mol. Mass.: | 15137.27 |
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| Organism: | Mus musculus (Mouse) |
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| Description: | Q05816 |
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| Residue: | 135 |
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| Sequence: | MASLKDLEGKWRLMESHGFEEYMKELGVGLALRKMAAMAKPDCIITCDGNNITVKTESTV
KTTVFSCNLGEKFDETTADGRKTETVCTFQDGALVQHQQWDGKESTITRKLKDGKMIVEC
VMNNATCTRVYEKVQ
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| Component 2 |
| Name | BDBM60927 |
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| Synonyms: | 1-anilinonaphthalene-8-sulfonic acid | 8-Anilino-1-naphthalenesulfonic acid | ANS | Anilinonaphthalene-8-sulfonic acid (ANS) | BDBM50126831 |
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| Type | n/a |
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| Emp. Form. | C16H13NO3S |
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| Mol. Mass. | 299.344 |
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| SMILES | OS(=O)(=O)c1cccc2cccc(Nc3ccccc3)c12 |
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| Structure | 
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| BDBM22988 |
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| n/a |
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| Name | BDBM22988 |
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| Synonyms: | (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide | AEA | ANANDAMIDE | Arachidonoyl ethanolamide | Arachidonoyl ethanolamide (AEA) | Arachidonoylethanolamide (AEA) | Arachidonylethanolamide | CHEMBL15848 | [14C]Anandamide | [3H]Anandamide |
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| Type | radiolabeled substrate |
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| Emp. Form. | C22H37NO2 |
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| Mol. Mass. | 347.5347 |
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| SMILES | CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)NCCO |
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| Structure | 
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