MDL29,951 | GPR17 activator
NMR: (Conforms)
Available Options
| Size : | Price | Quantity | |
|---|---|---|---|
| 5 mg | $85.00 | ||
| 25 mg | $300.00 |
MDL29,951 (130798-51-5) is a highly specific, small molecule activator of GPR17 that has been shown to be active in intact cells.1 The ability to specifically activate GPR17 allows for the study of the exact role GPR17 plays in the maturation of oligodendrocytes and may lead to a therapeutic strategy to promote myelin repair. MDL29,951 is antagonist for the strychnine-insensitive glycine binding site of the NMDA receptor (IC50 = 170 nM).2
References/Citations:
1) Hennen et al. (2013), Decoding Signaling and Function of the Orphan Protein-Coupled Receptor GPR17 with a small molecule agonist; Sci. Signal., 6 ra93
2) Salituro et al. (1992) 3-(2-Carboxyindol-3-yl)propionic Acid-Based Antagonists of the N-Methyl-D-aspartic Acid Receptor Associated Glycine Binding Site; J. Med. Chem., 35 1791
NMR: (Conforms)
Safety Data Sheet:
Product Data Sheet:
Materials provided by Focus Biomolecules are for laboratory research use only and are not intended for human or veterinary applications. Please note that we do not sell to individuals and that all orders placed by non-research organizations will incur a $20 restocking/refund fee
MDL29,951 (130798-51-5) is a highly specific, small molecule activator of GPR17 that has been shown to be active in intact cells.1 The ability to specifically activate GPR17 allows for the study of the exact role GPR17 plays in the maturation of oligodendrocytes and may lead to a therapeutic strategy to promote myelin repair. MDL29,951 is antagonist for the strychnine-insensitive glycine binding site of the NMDA receptor (IC50 = 170 nM).2
References/Citations:
1) Hennen et al. (2013), Decoding Signaling and Function of the Orphan Protein-Coupled Receptor GPR17 with a small molecule agonist; Sci. Signal., 6 ra93
2) Salituro et al. (1992) 3-(2-Carboxyindol-3-yl)propionic Acid-Based Antagonists of the N-Methyl-D-aspartic Acid Receptor Associated Glycine Binding Site; J. Med. Chem., 35 1791
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