- Cat. No.
- A15291
Ac-LEHD-AFC
Ac-LEHD-AFC, fluorogenic caspase substrate. Analog of the caspase-9 substrate, LEHD-AFC.
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Caspase inhibitors and activators act on cysteine proteases that cleave their substrates after aspartate residues. Initiator caspases such as caspase-8 and caspase-9 activate executioner caspases, including caspase-3, to dismantle the cell during apoptosis. Caspase-1, the first family member, was identified in 1992 as the protease that processes interleukin-1β (IL-1β). Peptide fluoromethyl ketones (FMKs) are the classic inhibitor type, led by the pan-caspase inhibitor Z-VAD-FMK. Z-DEVD-FMK, Z-IETD-FMK and Z-LEHD-FMK prefer caspase-3, caspase-8 and caspase-9, respectively. Q-VD-OPh is a broad caspase inhibitor, and belnacasan inhibits the inflammatory caspases 1 and 4. PAC-1 works in the opposite direction, as a small molecule that activates procaspase-3.
Ac-LEHD-AFC, fluorogenic caspase substrate. Analog of the caspase-9 substrate, LEHD-AFC.
Ac-LEHD-AFC is a fluorogenic substrate for caspase-4, caspase-5, and caspase-9.
Ac-YVAD-pNA is a specific Caspase-1 substrate. Ac-YVAD-pNA can be used to detect Caspase-1 activity. Caspase-1 is a key mediator of inflammatory processes.
Ac-LEVDGWK(Dnp)-NH2 is a synthetic substrate for Caspase-3, designed to facilitate the measurement of Caspase-3 enzymatic activity. Its use in research enables the study of apoptosis and cellular signaling pathways, providing insights into the role of Caspase-3 in various biological processes. This substrate can be employed in assays to quantify Caspase-3 activity in different biological samples.
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Z-VAD-AMC is a potent substrate for caspase-9, facilitating the study of apoptosis mechanisms. It exhibits high specificity for this caspase, enabling accurate monitoring of caspase activity in cellular assays. Researchers commonly utilize Z-VAD-AMC in studies focusing on programmed cell death, cellular stress responses, and therapeutic interventions targeting apoptotic pathways.
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Synonyms: D2R; (D)2-Rhodamine 110
(Asp)2-Rhodamine 110 is a fluorescent substrate specifically designed for caspase activity detection. This compound is cleaved by active caspases, resulting in the release of a fluorescent signal that allows for real-time monitoring of apoptosis in various biological systems. It is widely utilized in research applications focused on cell death mechanisms and therapeutic interventions targeting apoptosis.
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Ac-VDVAD-pNA is a specific substrate for caspase-2, designed to facilitate the assessment of caspase-2 activity in various biological samples. This reagent releases a chromogenic product upon cleavage by active caspase-2, making it useful for both in vitro and in vivo studies. It serves as a vital tool in research applications focused on apoptotic pathways and caspase-related signaling mechanisms.
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Synonyms: AC-WEHD-AMC
Ac-Trp-Glu-His-Asp-AMC is a specific fluorogenic substrate designed for caspase-1 detection and activity measurement. This compound exhibits high sensitivity and selectivity for caspase-1, enabling the quantitative assessment of apoptotic processes and inflammatory pathways. Its application in fluorescence assays facilitates the study of caspase-1's role in various biological contexts, including immune responses and cell death mechanisms.
Synonyms: Z-Ile-Glu-Thr-Asp-pNA
Z-IETD-pNA is a specific substrate for caspase-8 and granzyme B, designed for colorimetric detection. Upon hydrolysis by caspase-8, this compound releases para-nitroaniline (pNA), facilitating the measurement of enzyme activity. It is widely utilized in research applications focusing on apoptosis and immune responses, enabling the study of cell death mechanisms and the role of granzyme B in cytotoxicity.
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Synonyms: Z-Tyr-Val-Ala-Asp-pNA
Z-YVAD-pNA (Z-Tyr-Val-Ala-Asp-pNA) is a substrate specifically designed for caspase-1 activity. This compound is pivotal in studying inflammation and cell death pathways, as it is cleaved by caspase-1 during the activation of inflammatory caspases. Z-YVAD-pNA serves as an essential tool in research focused on apoptosis, pyroptosis, and other caspase-related signaling mechanisms. Its use can aid in the development of therapeutic strategies targeting inflammatory diseases.
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Ac-WEHD-AFC is a fluorogenic substrate specifically designed for the detection of caspase-1 activity. This compound enables the quantitative measurement of caspase-1 enzymatic function, making it a valuable tool in studies related to tumorigenesis and inflammatory processes. Its sensitive fluorescence readout facilitates the assessment of caspase-1 involvement in various biological systems.
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Ac-Asp-Glu-Val-Asp-pNA is a specific substrate for caspase-3/7, facilitating the study of apoptosis and cellular signaling pathways. This peptidic compound is cleaved by caspase-3/7, resulting in the release of p-nitroaniline (pNA), which can be quantitatively measured. Its use is critical in research applications focused on understanding programmed cell death and evaluating the activity of caspases in various biological contexts.
Ac-VDQQD-pNA is a selective substrate for Caspase 2, designed to facilitate the study of caspase activity. Upon cleavage by Caspase 2, it yields a yellow chromophore, p-nitroaniline (pNA), which can be quantitatively measured. This reagent is ideal for research applications focused on apoptosis, cell signaling, and the functional characterization of caspases.
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Mca-YVADAP-Lys(Dnp)-OH is a fluorogenic substrate designed for the characterization of caspase-1 and angiotensin-converting enzyme 2 (ACE2) activity. This compound enables the detection of enzymatic activity through fluorescence, making it valuable for studies focused on apoptosis and cardiovascular signaling pathways. It is suitable for use in various assays aimed at exploring the roles of these enzymes in cellular processes and disease states.
Ac-VEID-pNA serves as a substrate for caspase 6, specifically designed to facilitate the study of this protease's activity. By incorporating the VEID sequence, this synthetic peptide allows for the assessment of caspase 6-mediated cleavage events, particularly in the context of lamin A protein processing. It is valuable in research applications focusing on apoptosis and cell cycle regulation, contributing to a deeper understanding of cellular mechanisms and caspase involvement in various disease states.
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Ac-VEID-AFC is a fluorogenic substrate specifically designed for the detection of caspase-6 activity. Its cleavage by caspase-6 produces a fluorescent signal, making it a valuable tool for assessing apoptotic processes and related signaling pathways in various biological systems. This substrate is widely utilized in research applications focused on cell death, inflammation, and neurodegenerative diseases.
Ac-VRPR-AMC is a fluorogenic substrate specifically designed for the detection of metacaspase activity. This compound is utilized in biochemical assays to measure metacaspase activity, making it a valuable tool for research in apoptosis and programmed cell death. Its fluorescence properties enable sensitive detection, facilitating studies on metacaspase function in various biological systems.
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Ac-LEVD-pNA is a chromogenic substrate that specifically targets caspase-4, facilitating the detection of its enzymatic activity. This compound is essential for studies related to apoptosis and cellular signaling pathways, providing a reliable assay tool for researchers investigating caspase-mediated processes in various biological contexts.
Ac-DEVD-AFC is a fluorogenic substrate specifically designed for the detection of caspase-3 activity. Upon cleavage by caspase-3, it releases a fluorescent signal, enabling real-time monitoring of apoptosis. This reagent is widely used in cell biology research to evaluate programmed cell death and assess therapeutic effectiveness in various experimental settings.
Ac-YVAD-AFC is a fluorometric peptide substrate specifically targeting caspase-1 and caspase-4. It exhibits an excitation wavelength of 400 nm and an emission wavelength of 505 nm, making it suitable for assessing caspase activity in various biological samples. This compound is commonly used in research applications focused on apoptosis, inflammation, and disease mechanisms involving these caspases.
IETDC is a specific substrate for caspase 8, designed to monitor its activity through a bioluminescent assay. Upon cleavage by activated caspase 8, IETDC releases D-cysteine, which subsequently interacts with HCBT to generate firefly luciferin, producing a detectable bioluminescent signal. This reagent is particularly valuable for investigating acute inflammation and understanding the role of caspase 8 in apoptotic signaling pathways.
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Ac-IETD-AMC is a fluorogenic substrate specifically designed for the detection and quantification of caspase-8 activity. This compound, which includes an acetyl (Ac) moiety, serves as an efficient tool for studying apoptosis and related pathways mediated by caspase-8 and granzyme B. Its application in research allows for precise measurement of caspase-8 activity in various biological contexts, facilitating insights into cell death mechanisms and potential therapeutic targets.
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