Ac-DEVD-AFC | CAS 201608-14-2

Name: Ac-DEVD-AFC
Brand: BOC Sciences
Rating: 5 (1 reviews)

Catalog Number	A18-0003
Category	Fluorescent Enzyme Substrates
Molecular Formula	C30H34F3N5O13
Molecular Weight	729.61

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Product Introduction

Ac-DEVD-AFC is a synthetic peptide substrate widely utilized in biochemical assays to detect caspase-3 activity. This compound features an acetylated aspartic acid residue linked to a fluorogenic 7-amino-4-trifluoromethylcoumarin (AFC) moiety, which enables the monitoring of enzymatic cleavage events. Upon cleavage by caspase-3, the AFC group is released, emitting a fluorescent signal that is easily measurable. Researchers employ Ac-DEVD-AFC to gain insights into apoptotic pathways and cellular processes involving caspase activity.

Chemical Information
Product Specification
Application

Synonyms	Ac-DEVD-7-amido-4-trifluoroMethylcoumarin; Caspase-3 Substrate Ⅶ, Fluorogenic; Ac-Asp-Glu-Val-Asp-AFC; N-acetyl-L-α-aspartyl-L-α-glutamyl-L-valyl-N-[2-oxo-4-(trifluoromethyl)-2H-1-benzopyran-7-yl]-L-α-asparagine
Purity	≥90%
IUPAC Name	(4S)-4-[[(2S)-2-acetamido-3-carboxypropanoyl]amino]-5-[[(2S)-1-[[(2S)-3-carboxy-1-oxo-1-[[2-oxo-4-(trifluoromethyl)chromen-7-yl]amino]propan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-oxopentanoic acid
Canonical SMILES	CC(C)C(C(=O)NC(CC(=O)O)C(=O)NC1=CC2=C(C=C1)C(=CC(=O)O2)C(F)(F)F)NC(=O)C(CCC(=O)O)NC(=O)C(CC(=O)O)NC(=O)C
InChI	InChI=1S/C30H34F3N5O13/c1-12(2)25(38-26(47)17(6-7-21(40)41)36-28(49)18(10-22(42)43)34-13(3)39)29(50)37-19(11-23(44)45)27(48)35-14-4-5-15-16(30(31,32)33)9-24(46)51-20(15)8-14/h4-5,8-9,12,17-19,25H,6-7,10-11H2,1-3H3,(H,34,39)(H,35,48)(H,36,49)(H,37,50)(H,38,47)(H,40,41)(H,42,43)(H,44,45)/t17-,18-,19-,25-/m0/s1
InChIKey	GZDRODOYEFEHGG-NUDCOPPTSA-N
Solubility	Soluble in Water
Density	1.495±0.06 g/cm3 (Predicted)
Appearance	White Powder
Boiling Point	1152.7±65.0°C (Predicted)

Excitation	400 nm
Emission	505 nm
Storage	Store at -20°C

Ac-DEVD-AFC is primarily utilized in apoptosis research, specifically for detecting caspase activity. Caspases, a family of cysteine proteases, play a critical role in programmed cell death. The substrate Ac-DEVD-AFC is designed to be selectively cleaved by caspase-3, one of the key effectors in the apoptosis pathway. By incorporating a fluorophore, this substrate enables researchers to monitor caspase-3 activity in real-time through fluorescence. This application is crucial for understanding the mechanisms of apoptosis and can aid in the development of therapies targeting cancer and neurodegenerative diseases, where dysregulation of apoptosis is a significant concern.

Another important application of Ac-DEVD-AFC is in drug discovery and development. By measuring the activity of caspase-3 in various cell lines treated with potential drug candidates, researchers can evaluate the pro-apoptotic effects of these compounds. This high-throughput screening method allows for the rapid identification of drugs that can induce apoptosis in cancer cells. Additionally, Ac-DEVD-AFC can be used to assess the efficacy of combination therapies, enhancing the understanding of drug interactions and synergistic effects in cancer treatment. This application underscores the substrate's role in advancing therapeutic strategies and improving patient outcomes.

Ac-DEVD-AFC is also instrumental in toxicology studies. It serves as a valuable tool for assessing the cytotoxic effects of environmental pollutants, chemicals, or pharmaceuticals on cellular systems. By measuring caspase-3 activity in cells exposed to these agents, researchers can determine the extent of apoptosis induced by toxic substances. This information is vital for regulatory assessments and risk evaluations, helping to establish safety profiles for various compounds. Furthermore, understanding the mechanisms of toxicity can inform the development of safer alternatives and improve environmental health.

Lastly, Ac-DEVD-AFC finds application in fundamental cell biology research, particularly in studies examining the regulation of apoptosis. Researchers can utilize this substrate to explore how various cellular signaling pathways influence caspase activation and activity. By manipulating factors such as growth factors, cytokines, and stressors, scientists can elucidate the intricate networks that govern cell survival and death. This knowledge is essential for developing strategies to manipulate apoptosis in various diseases, including cancer, autoimmune disorders, and degenerative diseases. The insights gained from these studies can lead to innovative therapeutic approaches that harness or inhibit apoptosis for clinical benefit.