ALEXIS Biochemicals: BAY 60-7550

ALX-270-421

Revised 14-Feb-07

BAY 60-7550
SYNONYMS	2-(3,4-Dimethoxybenzyl)-7-[(1R)-1-[(1R)-1-hydroxyethyl]-4-phenylbutyl]-5-methylimidazo[5,1-f][1,2,4]triazin-4(3H)-one
PRODUCT LINE	Signal Transduction
PRODUCT CATEGORY	Phosphodiesterases / Related Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-270-421-M005		5 mg	98.00 USD
ALX-270-421-M025		25 mg	395.00 USD

Product Specification

FORMULA:	C₂₇H₃₂N₄O₄
MW:	476.6
PURITY:	≥97% (HPLC)
APPEARANCE:	White to off-white powder.
SOLUBILITY:	Soluble in acetone, DMSO or 100% ethanol. Insoluble in water.
SHIPPING:	AMBIENT
LONG TERM STORAGE:	+4°C

Product Description

Inhibitor of human phosphodiesterase 2 (PDE2) (IC₅₀=5nM). Selective (>50-fold) versus other human PDEs tested (1C,3A, 4B, 5A, 6, 7B, 8A, 9A, 10A, 11A) and does not affect adenosine deaminase. Raises cGMP levels in cell culture, particularly in combination with a suitable activator of soluble guanylyl cyclase (sGC). Raises cAMP in combination with forskolin (Prod. No. ALX-350-001). Increases memory performance in rodents in vivo.

Product Specific Literature References

Inhibition of phosphodiesterase 2 increases neuronal cGMP, synaptic plasticity and memory performance: F.G. Boess, et al.; Neuropharmacology 47, 1081 (2004) Abstract

General Information

BACKGROUND/TECHNICAL INFORMATION

Please also see our Product Flyer "BAY 60-7550 - A Novel Potent & Selective PDE2 Inhibitor".

General Literature References

Dynamic regulation of cAMP signaling by cGMP in the cardiovascular system: roles of phosphodiesterase 2 and phosphodiesterase 3 enzymes: D.H. Maurice; Proc. West. Pharmacol. Soc. 46, 32 (2003) Abstract
Cyclic nucleotide phosphodiesterases and their role in immunomodulatory responses: advances in the development of specific phosphodiesterase inhibitors: A. Castro, et al.; Med. Res. Rev. 25, 229 (2005) Abstract
The next generation of phosphodiesterase inhibitors: structural clues to ligand and substrate selectivity of phosphodiesterases: D.T. Manallack, et al.; J. Med. Chem. 48, 3449 (2005) Abstract