Z-VAD(OMe)-FMK (Z-Val-Ala-Asp(OMe)-FMK) is a cell-permeable and irreversible pan-caspase inhibitor. Z-VAD(OMe)-FMK is an ubiquitin carboxy-terminal hydrolase L1 (UCHL1) inhibitor. Z-VAD(OMe)-FMK irreversibly modifies UCHL1 by targeting the active site of UCHL1.
CAT No: R1807
CAS No:187389-52-2
Synonyms/Alias:187389-52-2;Z-VAD(OMe)-FMK;Z-Val-Ala-Asp(OMe)-FMK;pan-caspase inhibitor;C22H30FN3O7;ZVAD-FMK;5-Bromo-2 -deoxyuridine;Z-VAD (OMe)-FMK;Z-Val-Ala-Asp(OMe)-fluoromethyl ketone;Z-Val-Ala-Asp(OMe)-CH2F;methyl (3S)-5-fluoro-3-[[(2S)-2-[[(2S)-3-methyl-2-(phenylmethoxycarbonylamino)butanoyl]amino]propanoyl]amino]-4-oxopentanoate;Benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone;z-Val-Ala-Asp(OMe)-fluoromethylketone;methyl (5S,8S,11S)-11-(2-fluoroacetyl)-5-isopropyl-8-methyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazatridecan-13-oate;methyl 5-fluoro-3-[2-[[3-methyl-2-(phenylmethoxycarbonylamino)butanoyl]amino]propanoylamino]-4-oxopentanoate;Z-Val-Ala-Asp(OCH3)-fluoromethylketone;L-alaninamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-3-fluoro-1-(2-methoxy-2-oxoethyl)-2-oxopropyl]-;METHYL (3S)-3-[(2S)-2-[(2S)-2-{[(BENZYLOXY)CARBONYL]AMINO}-3-METHYLBUTANAMIDO]PROPANAMIDO]-5-FLUORO-4-OXOPENTANOATE;benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethyl ketone;N-benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone;N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone;MFCD02684037;Bio2_000471;Z-VAD(OMe)-FMK?;Z-VAD-(OMe)-FMK;Probes1_000501;CBiol_001923;BSPBio_001262;KBioGR_000602;KBioSS_000602;Caspase-1 Inhibitor Z-Val-Ala-DL-Asp-fluoromethylketone;CHEMBL1213366;SCHEMBL15012737;Z-Val-Ala-Asp(OCH3)-CH2F;KBio2_000602;KBio2_003170;KBio2_005738;KBio3_001063;KBio3_001064;DTXSID40420586;CHEBI:137045;Bio1_000209;Bio1_000698;Bio1_001187;Bio2_000951;HMS1362P03;HMS1792P03;HMS1990P03;HMS3403P03;EX-A2192;HB1285;HB1319;Z-L-Val-L-Ala-L-Asp(OMe)-CH2F;AKOS024456966;z-Val-Ala-Asp(OMe) fluoromethylketone;CCG-207882;CS-3153;IDI1_002226;z-Val-Ala-Asp(OMe)-fluoromethyl-ketone;Cbz-Val-Ala-Asp(OMe)-fluoromethylketone;NCGC00163487-01;NCGC00163487-02;AS-74918;Cbz-Val-Ala-Asp(OMe)-fluoromethyl ketone;HY-16658;Z-Val-Ala-Asp(OCH3)-fluoromethyl ketone;z-Val-Ala-Asp(O-methyl)-fluoromethylketone;SW219162-1;Caspase Inhibitor I - CAS 187389-52-2;Z-VAD(OMe)-FMK; Z-Val-Ala-Asp(OMe)-FMK;benzyloxycarbonyl-Val-Ala-Asp(OMe) fluoromethyl ketone;benzyloxycarbonyl-Val-Ala-Asp(OMe)fluoromethyl ketone;N-benzyloxycarbonyl-Val-Ala-Asp(OMe)fluoromethylketone;benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone;N-benzyloxycarbonyl-Val-Ala-Asp(OMe) fluoromethyl ketone;N-benzyloxycarbonyl-Val-Ala-Asp(OMe) fluoromethylketone;N-benzyloxycarbonyl-Val-Ala-Asp(OMe)fluoromethyl ketone;benzyloxycarbonyl-Val-Ala-Asp(O-methyl)-fluoromethylketone;N-benzyloxycarbonyl-Val-Ala-Asp(O-methyl) fluoromethyl ketone;N-benzyloxycarbonyl-Val-Ala-Asp(O-methyl)-fluoromethyl ketone;N-benzyloxycarbonyl-Val-Ala-Asp(O-methyl)-fluoromethylketone;(5S,8S,11S)-Methyl 11-(2-fluoroacetyl)-5-isopropyl-8-methyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazatridecan-13-oate;L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-3-fluoro-1-(2-methoxy-2-oxoethyl)-2-oxopropyl]- (9CI);N-[(benzyloxy)carbonyl]-L-valyl-N-[(3S)-5-fluoro-1-methoxy-1,4-dioxopentan-3-yl]-L-alaninamide;
Caspase Inhibitor I is a synthetic small-molecule compound widely recognized for its ability to modulate caspase activity in biochemical and cellular systems. As a potent, cell-permeable inhibitor targeting a broad range of caspases, it plays a crucial role in apoptosis research and the investigation of programmed cell death pathways. Its specificity and reversible binding characteristics make it an indispensable tool for dissecting the molecular mechanisms underlying caspase activation, substrate cleavage, and downstream signaling events. Researchers value its functional significance in studies involving cell fate decisions, stress responses, and the regulation of inflammation, positioning it as a foundational reagent in both basic and applied life science investigations.
Apoptosis research: Caspase Inhibitor I is extensively utilized in the study of apoptotic mechanisms, enabling precise dissection of caspase-dependent cell death pathways. By selectively inhibiting caspase activity, it allows researchers to distinguish between caspase-mediated and alternative forms of cell death, such as necrosis or autophagy. This mechanistic clarity is essential for mapping the sequence of molecular events during apoptosis, identifying critical regulatory nodes, and validating the involvement of specific caspases in response to various stimuli. Its use supports the development of robust experimental models for elucidating the cellular consequences of caspase inhibition in diverse biological contexts.
Cell signaling pathway analysis: The compound serves as a valuable tool for probing the intricate network of cell signaling pathways that intersect with caspase activation. By blocking caspase-mediated proteolysis, investigators are able to assess the impact of caspase inhibition on downstream effectors, including transcription factors, kinases, and other signaling proteins. This approach is instrumental in unraveling the cross-talk between apoptosis and other cellular processes, such as cell proliferation, differentiation, and immune responses. The ability to modulate caspase activity with high temporal control provides insight into the dynamic regulation of signaling cascades during physiological and stress-induced conditions.
Inflammation studies: Caspase Inhibitor I is frequently applied in research focused on the regulation of inflammatory processes, particularly those involving caspase-1 and the maturation of pro-inflammatory cytokines such as interleukin-1β. By suppressing caspase activity, it aids in delineating the molecular mechanisms governing inflammasome assembly, cytokine processing, and the initiation of inflammatory cell death (pyroptosis). This functional relevance extends to experimental models investigating the interplay between cell death and innate immune signaling, facilitating a deeper understanding of the molecular underpinnings of inflammation and immune regulation.
Protease substrate validation: The inhibitor is also employed in the validation of putative caspase substrates, enabling researchers to confirm whether specific proteins are direct targets of caspase cleavage during apoptosis or related processes. By comparing substrate cleavage patterns in the presence and absence of the inhibitor, investigators can map caspase recognition motifs, characterize cleavage kinetics, and identify novel substrates. This application is essential for expanding the repertoire of known caspase substrates and for understanding the broader consequences of caspase activity on cellular proteomes.
Drug discovery and screening: In pharmaceutical and biotechnology research, Caspase Inhibitor I is leveraged in high-throughput screening assays to evaluate the efficacy of novel compounds targeting apoptotic pathways. Its use as a reference inhibitor provides a benchmark for assessing the specificity and potency of candidate molecules, supporting the identification and optimization of new chemical entities with potential to modulate cell death mechanisms. By establishing reliable assay controls, it contributes to the development of robust screening platforms for apoptosis-related targets, thereby accelerating the discovery pipeline for research-use compounds and pathway modulators.
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