Q-VD-OPH is a broad-spectrum caspase inhibitor that blocks caspases-3, -7, -8, -9, -10, and -12. It more effectively inhibits apoptosis and is much less cytotoxic than Z-VAD-FMK and Boc-D-FMK.
CAT No: R0812
CAS No:1135695-98-5
Synonyms/Alias:1135695-98-5;Q-VD-OPh;Q-VD-OPh hydrate;QVD-OPH;(3S)-5-(2,6-Difluorophenoxy)-3-[[(2S)-3-methyl-1-oxo-2-[(2-quinolinylcarbonyl)amino]butyl]amino]-4-oxo-pentanoic Acid;(3S)-5-(2,6-difluorophenoxy)-3-[[(2S)-3-methyl-2-(quinoline-2-carbonylamino)butanoyl]amino]-4-oxopentanoic acid;(S)-5-(2,6-Difluorophenoxy)-3-((S)-3-methyl-2-(quinoline-2-carboxamido)butanamido)-4-oxopentanoic acid;N-(2-Quinolyl)valyl-aspartyl-(2,6-difluorophenoxy)methyl ketone;pentanoic acid, 5-(2,6-difluorophenoxy)-3-[[(2S)-3-methyl-1-oxo-2-[(2-quinolinylcarbonyl)amino]butyl]amino]-4-oxo-, (3S)-;Quinoline-Val-Asp-Difluorophenoxymethylketone;MFCD08669741;CHEMBL4237988;SCHEMBL15449978;DTXSID90647322;C26H25F2N3O6;CHEBI:232611;EX-A1093;s7311;AKOS027446655;CCG-269797;CS-6252;AC-31505;BS-14641;FD103285;HY-12305;N-(2-Quinolinyl)valyl-aspartyl (2,6-difluorophenoxy)methyl ketone;(3S)-5-(2,6-DIFLUOROPHENOXY)-3-[(2S)-3-METHYL-2-(QUINOLIN-2-YLFORMAMIDO)BUTANAMIDO]-4-OXOPENTANOIC ACID;(3S)-5-(2,6-Difluorophenoxy)-4-oxo-3-{[N-(quinoline-2-carbonyl)-L-valyl]amino}pentanoic acid;
Q-VD-OPH is a synthetic, cell-permeable pan-caspase inhibitor widely used in biochemical and cell biology research to study apoptotic pathways and cell death mechanisms. As a potent and irreversible inhibitor, it functions by covalently binding to the active site cysteine of caspases, thereby blocking the proteolytic activity required for the execution phase of apoptosis. Its chemical structure, designed to enhance metabolic stability and minimize cytotoxicity compared to earlier caspase inhibitors, makes it particularly valuable for experiments requiring prolonged inhibition of caspase activity. Q-VD-OPH has become a preferred tool for dissecting the molecular underpinnings of programmed cell death, enabling researchers to differentiate between caspase-dependent and caspase-independent processes in diverse cellular systems.
Apoptosis research: In studies focused on programmed cell death, Q-VD-OPH is frequently employed to inhibit caspase activation and thereby prevent the characteristic morphological and biochemical changes associated with apoptosis. By blocking the cleavage of caspase substrates, the compound allows researchers to delineate the contribution of caspase-mediated pathways to cellular demise. Its high specificity and low off-target toxicity enable precise interrogation of apoptotic signaling in a variety of mammalian cell types, including primary cells and established lines.
Neuroprotection studies: The compound is widely utilized in neuroscience research to investigate neuronal survival and the mechanisms underlying neurodegeneration. By inhibiting caspase activity, Q-VD-OPH helps determine the extent to which apoptotic processes contribute to neuronal cell loss in models of traumatic injury, oxidative stress, or excitotoxicity. Its use facilitates the exploration of alternative, non-apoptotic modes of cell death and supports the development of neuroprotective strategies in preclinical models.
Cell culture viability assays: In cell-based experiments, Q-VD-OPH is often incorporated into culture systems to preserve cell viability during exposure to stressors or cytotoxic agents. By preventing caspase-driven apoptosis, the compound enables extended observation periods and more accurate assessment of cellular responses to experimental manipulations. Its compatibility with a range of cell types and minimal impact on cell proliferation make it a reliable choice for optimizing assay conditions in high-content screening or long-term studies.
Inflammation and immune response analysis: The inhibitor is also applied in immunology to dissect the role of caspases in inflammatory cell death pathways such as pyroptosis. By selectively blocking caspase activity, investigators can distinguish between apoptosis, necroptosis, and pyroptosis, clarifying the molecular mechanisms underlying immune cell activation, cytokine release, and tissue injury. This application is particularly relevant in studies of innate immunity and inflammatory disease models.
Protease pathway mapping: Q-VD-OPH serves as a valuable tool for mapping protease networks in complex biological systems. Its ability to irreversibly inhibit a broad spectrum of caspases allows for the identification of caspase substrates and the temporal sequence of proteolytic events during cell death. Researchers leverage this property to elucidate cross-talk between protease families, uncover novel regulatory mechanisms, and validate potential targets for further biochemical characterization.
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