Biotin-YVAD-FMK

Biotin-YVAD-FMK features a YVAD motif and FMK electrophile tethered to a biotin label. The peptide binds and covalently modifies proteases recognizing this canonical sequence. Researchers use it in affinity enrichment, active-site mapping, and inhibitory profiling. Its multifunctional design supports sensitive detection and mechanistic evaluation.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: HB00047

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cGMP Peptide
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M.F/Formula
C33H47FN6O9S
M.W/Mr.
722.8304
Purity
95/98%

Biotin-YVAD-FMK is a synthetic peptide inhibitor designed for the selective and irreversible inhibition of caspase-1, a cysteine protease central to the regulation of inflammation and pyroptosis. Structurally, it comprises the biotinylated tetrapeptide sequence Tyr-Val-Ala-Asp (YVAD) linked to a fluoromethyl ketone (FMK) warhead, conferring specificity for caspase-1's active site. The inclusion of a biotin moiety enables facile detection and affinity-based isolation, enhancing its versatility in biochemical assays and cell-based studies. Owing to its dual functionality as both a probe and an inhibitor, Biotin-YVAD-FMK is widely utilized in the investigation of inflammasome signaling, protease activity profiling, and the molecular mechanisms underlying programmed cell death.

Inflammasome research: As a potent and selective caspase-1 inhibitor, Biotin-YVAD-FMK is routinely employed to dissect the molecular events governing inflammasome activation. Researchers utilize this compound to block caspase-1-mediated maturation of pro-inflammatory cytokines such as interleukin-1β and interleukin-18, thereby enabling precise evaluation of inflammasome-dependent signaling pathways. Its application in in vitro and cell-based assays allows for the elucidation of upstream and downstream components involved in innate immune responses and inflammatory disease models.

Protease activity profiling: The biotin tag incorporated into the peptide sequence facilitates the affinity capture and subsequent identification of active caspase-1 in complex biological samples. By enabling the selective labeling and isolation of enzymatically active protease populations, Biotin-YVAD-FMK supports detailed proteomic analyses and the mapping of caspase-1 substrates. This approach is instrumental in characterizing protease function, substrate specificity, and the broader landscape of cysteine protease activities within cellular environments.

Cell death pathway analysis: In studies of pyroptosis and related forms of programmed cell death, Biotin-YVAD-FMK serves as a valuable tool for delineating the specific contributions of caspase-1. By inhibiting its proteolytic activity, researchers can distinguish caspase-1-dependent cell death from apoptosis or necroptosis, thereby clarifying the mechanistic underpinnings of cell fate decisions. The compound's utility in both biochemical and cellular models enhances the resolution of pathway-specific investigations.

Affinity-based detection: The biotinylated nature of this peptide inhibitor enables its use in a range of affinity-based techniques, including Western blotting, immunoprecipitation, and pull-down assays. By leveraging streptavidin or avidin conjugates, scientists can visualize, quantify, or isolate caspase-1 and its interacting partners with high specificity. This capability is particularly valuable for monitoring enzyme activation, validating target engagement, and supporting downstream analytical workflows.

Drug discovery and inhibitor screening: Biotin-YVAD-FMK is frequently utilized in the development and validation of new caspase-1 inhibitors. Its well-characterized inhibitory profile and amenability to high-throughput screening platforms make it an ideal positive control or benchmarking compound in enzymatic assays. Furthermore, its application in competitive binding studies aids in the identification and optimization of novel small-molecule modulators targeting inflammatory caspases, supporting the advancement of anti-inflammatory research and therapeutic innovation.

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