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AB120030

(S)-(+)-Rolipram,PDE4抑制剂

(S)-(+)-Rolipram, PDE4 inhibitor

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(1 Publication)

MW 275.34 Da, Purity >99%. PDE4 inhibitor (IC50 = 0.58 μM). Less active enantiomer. Achieve your results faster with highly validated, pure and trusted compounds.

查看别名

2EL, 5''-cyclic phosphodiesterase 4A, 5''-cyclic phosphodiesterase 4B, 5''-cyclic phosphodiesterase 4C, 5''-cyclic phosphodiesterase 4D, DKFZp686F2182, DKFZp686M11213, DPDE 1, DPDE2, DPDE3, DPDE4, Dunce like phosphodiesterase E3, FLJ97311, HSPDE4D, MGC126222, MGC126529, OTTHUMP00000010652, OTTHUMP00000010653, OTTHUMP00000010654, OTTHUMP00000010656, OTTHUMP00000232365, PDE 21, PDE IVB, PDE32, PDE4, PDE43, PDE46, PDE4A11, PDE4A_HUMAN, PDE4B5, PDE4B_HUMAN, PDE4C_HUMAN, PDE4DN2, PDE4D_HUMAN, Phosphodiesterase 4A, Phosphodiesterase 4A, cAMP-specific (dunce, Phosphodiesterase 4B, Phosphodiesterase 4B cAMP specific, Phosphodiesterase 4B, cAMP specific (phosphodiesterase E4 dunce homolog, Drosophila), Phosphodiesterase 4C, Phosphodiesterase 4C cAMP specific, Phosphodiesterase 4C, cAMP specific (phosphodiesterase E1 dunce homolog, Drosophila), Phosphodiesterase 4D cAMP specific (dunce (Drosophila) homolog phosphodiesterase E3), Phosphodiesterase 4D cAMP specific (phosphodiesterase E3 dunce homolog Drosophila), Phosphodiesterase 4D cAMP-specific, Phosphodiesterase 4D, cAMP specific (dunce), Phosphodiesterase E1 dunce homolog, Phosphodiesterase E1 dunce homolog Drosophila, Phosphodiesterase E2 dunce homolog, Drosophila, Phosphodiesterase type 4C, STRK1, cAMP specific 3' 5' cyclic phosphodiesterase 4C, cAMP specific 3',5' cyclic phosphodiesterase 4D, cAMP specific phosphodiesterase, cAMP specific phosphodiesterase 4D, cAMP specific phosphodiesterase PDE4D6, cAMP-specific 3'', cAMP-specific 3',5'-cyclic phosphodiesterase 4A, cAMP-specific 3',5'-cyclic phosphodiesterase 4B, cAMP-specific phosphodiesterase-4 B isoform, dunce like phosphodiesterase E2, dunce-like phosphodiesterase E4, phosphodiesterase 4A cAMP specific, phosphodiesterase E2 dunce homolog, phosphodiesterase isozyme 4, phosphodiesterase type 4A11

1 Images
Chemical Structure - (S)-(+)-Rolipram, PDE4 inhibitor (AB120030)
  • Chemical Structure

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Chemical Structure - (S)-(+)-Rolipram, PDE4 inhibitor (AB120030)

2D chemical structure image of ab120030, (S)-(+)-Rolipram, PDE4 inhibitor

关键信息

CAS 号

85416-73-5

纯度

>99%

形式

Solid

form

分子量

275.34 Da

分子式

C<sub>1</sub><sub>6</sub>H<sub>2</sub><sub>1</sub>NO<sub>3</sub>

PubChem

158758

属性

Synthetic

溶解度

Soluble in DMSO to 100 mM

生化试剂名称

(S)-(+)-rolipram

生物学描述

PDE4 inhibitor (IC50 = 0.58 μM). Less active enantiomer.

经典 SMILES

COC1=C(C=C(C=C1)C2CC(=O)NC2)OC3CCCC3

同分异构的 SMILES

COC1=C(C=C(C=C1)[C@@H]2CC(=O)NC2)OC3CCCC3

InChi

InChI=1S/C16H21NO3/c1-19-14-7-6-11(12-9-16(18)17-10-12)8-15(14)20-13-4-2-3-5-13/h6-8,12-13H,2-5,9-10H2,1H3,(H,17,18)/t12-/m1/s1

InChiKey

HJORMJIFDVBMOB-GFCCVEGCSA-N

IUPAC 名

(4S)-4-(3-cyclopentyloxy-4-methoxyphenyl)pyrrolidin-2-one

性能和储存信息

运输条件
Ambient - Can Ship with Ice
推荐的短期储存条件
+4°C
推荐的长期储存条件
+4°C
储存信息
Store under desiccating conditions|The product can be stored for up to 12 months

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

The PDE4 family including PDE4A PDE4B PDE4C and PDE4D constitutes a group of phosphodiesterases involved in cyclic AMP (cAMP) hydrolysis. PDE4 enzymes commonly referred to as cAMP-specific phosphodiesterases play a mechanical role by breaking down cAMP into AMP therefore regulating intracellular levels of cAMP. These enzymes vary in molecular mass with PDE4A ranging from approximately 66 to 85 kDa depending on isoform variants. Expression of PDE4 subtypes differs across tissues but they are widely expressed in the brain immune cells and smooth muscle tissues. Understanding their mechanical action allows targeting with PDE4 inhibitors which are relevant in various therapeutic areas.
Biological function summary

These PDE4 enzymes serve critical functions in modulating cellular responses to extracellular signals. By regulating cAMP levels they influence processes such as inflammation and smooth muscle contraction. PDE4 enzymes do not typically form part of large protein complexes but may interact with other proteins such as signaling scaffolds. Their ability to regulate cAMP a second messenger makes them important players in cellular signaling pathways. Each PDE4 subtype plays specialized roles depending on their expression patterns and local cellular environments.

Pathways

PDE4 enzymes critically impact the regulation of the cAMP signaling pathway and the MAPK/ERK pathway. cAMP is a pivotal signaling molecule in transferring hormonal signals into cellular responses. PDE4 enzymes modulate intracellular cAMP levels affecting processes like activation of protein kinase A (PKA) and cAMP-response element-binding protein (CREB). Relation exists between PDE4 and other proteins like EPAC which also bind cAMP to elicit distinct cellular responses. The modulation of MAPK/ERK pathway by PDE4 enzymes further integrates them into the wider network of cellular signal transduction.

PDE4 enzymes have links to inflammatory conditions and neuropsychiatric disorders like depression. By controlling cAMP levels PDE4 affects inflammatory responses relevant in conditions such as chronic obstructive pulmonary disease (COPD). PDE4 inhibitors show promise in managing inflammation by preventing excess cAMP breakdown. In the brain altered PDE4 activity influences mood regulation connecting it to proteins like CREB which play a role in neuroplasticity pivotal to depression management. Targeting specific PDE4 subtypes offers potential in developing treatments for these conditions.

产品实验方案

文献 (1)

Recent publications for all applications. Explore the full list and refine your search

OBM neurobiology 5: PubMed33521586

2021

N-type calcium channels control GABAergic transmission in brain areas related to fear and anxiety.

Applications

Unspecified application

Species

Unspecified reactive species

Maxwell Blazon,Brianna LaCarubba,Alexandra Bunda,Natalie Czepiel,Shayna Mallat,Laura Londrigan,Arturo Andrade
View all publications

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