Product Name: Caspase 1 (ICE) Inhibitor II, biotinylated
Sequence One Letter Code: Biotin-YVAD-CMK
Sequence Three Letter Code: Biotin-Tyr-Val-Ala-Asp-Chloromethyl Ketone
Chemical Formula:C32H45ClN6O9S
Molecular Weight: 725.3
Purity: 95%
Form: Lyophilized
Storage Conditions: - 20 °C
Research Area: Cancer Disease Research
Conjugation: Conjugated
Conjugation Type: Biotins
Code Nacres: NA.26
Application: Caspase-1 (ICE) Inhibitor II, biotinylated is an irreversible peptide inhibitor containing the YVAD recognition sequence linked to a chloromethyl ketone reactive group. N-terminal biotinylation enables affinity purification and detection applications. By covalently modifying the active-site cysteine, the inhibitor blocks caspase-1–mediated processing of pro-IL-1β and inflammasome signaling. It is widely used in inflammation and cell death research to evaluate caspase-1 function and downstream cytokine maturation. The compound supports mechanistic studies of pyroptosis and neuroinflammatory responses in vitro.
Current Research: Caspase-1 (ICE) Inhibitor II, biotinylated is an irreversible peptide-based inhibitor designed to selectively target caspase-1, historically referred to as interleukin-1β–converting enzyme (ICE). The inhibitor incorporates the canonical YVAD recognition sequence, which confers specificity for caspase-1, linked to a chloromethyl ketone (CMK) reactive group. This electrophilic warhead covalently modifies the catalytic cysteine residue within the caspase-1 active site, resulting in permanent enzyme inactivation. N-terminal biotinylation expands its utility by enabling affinity-based detection and purification strategies. Mechanism of Action Caspase-1 is a cysteine protease activated within multiprotein inflammasome complexes such as NLRP3, AIM2, and NLRC4. Upon activation, caspase-1 cleaves pro–IL-1β and pro–IL-18 into their mature, bioactive cytokine forms and initiates pyroptotic cell death through cleavage of gasdermin D. Caspase-1 (ICE) Inhibitor II functions by: Recognizing the YVAD substrate motif preferred by caspase-1 Covalently binding to the catalytic cysteine via the chloromethyl ketone group Preventing substrate cleavage and downstream cytokine maturation Because the inhibition is irreversible, the compound is particularly effective for mechanistic studies requiring sustained suppression of enzymatic activity. Role in Inflammasome and Pyroptosis Research Inflammasome activation is central to innate immune responses and inflammatory disease pathogenesis. By blocking caspase-1 activity, this inhibitor enables controlled evaluation of inflammasome-dependent processes, including: IL-1β and IL-18 maturation Gasdermin D cleavage Pyroptotic membrane pore formation Release of inflammatory mediators In cellular models, the inhibitor is commonly used to distinguish caspase-1–dependent effects from alternative inflammatory pathways. Applications in Neuroinflammation and Immunology Caspase-1 signaling has been implicated in neuroinflammatory disorders, metabolic inflammation, sepsis, and autoimmune disease models. Caspase-1 (ICE) Inhibitor II, biotinylated is widely applied in: Inflammasome activation assays Cytokine secretion analysis Neuroinflammation studies in microglial or neuronal cultures Evaluation of small-molecule inflammasome modulators Pyroptosis pathway investigations Its defined specificity for the YVAD motif supports selective inhibition within experimental systems. Biotinylation and Affinity Applications The N-terminal biotin tag enables high-affinity interaction with streptavidin or avidin platforms, supporting: Pull-down assays to identify caspase-1 complexes Detection of inhibitor-bound enzyme Affinity purification of inflammasome components Quantitative binding and occupancy studies This functionality allows researchers to combine enzymatic inhibition with biochemical tracking and protein interaction mapping. Experimental Advantages Irreversible covalent inhibition of caspase-1 YVAD sequence conferring substrate specificity Chloromethyl ketone reactive group for active-site targeting Biotin modification enabling affinity capture and detection Suitable for biochemical and cell-based inflammasome assays Research Significance Caspase-1 (ICE) Inhibitor II, biotinylated provides a powerful tool for dissecting inflammasome signaling and caspase-1–mediated cytokine maturation. By enabling irreversible enzyme blockade alongside affinity-based detection, it supports detailed mechanistic investigation of pyroptosis, inflammatory signaling cascades, and neuroimmune interactions in vitro. Its combined specificity and functional tagging make it particularly valuable in immunology and inflammation research.
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