Flagelin 22(TFA)

Flagelin 22 TFA (Flagellin 22 TFA), a fragment of bacterial flagellin, is an effective elicitor in both plants and algae.

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

CAT No: R1357

Synonyms/Alias:Flagellin 22(TFA)

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M.F/Formula
C₉₅H₁₆₃F₃N₃₂O₃₆
M.W/Mr.
2386.50

Flagelin 22(TFA) is a synthetic peptide derived from the conserved N-terminal domain of bacterial flagellin, a principal structural protein of the flagellar filament. As a well-characterized microbe-associated molecular pattern (MAMP), this peptide is recognized by plant pattern recognition receptors, notably FLS2, triggering robust immune signaling cascades. Its biochemical significance lies in its ability to mimic native flagellin epitopes, making it a valuable molecular tool for dissecting plant innate immunity, receptor-ligand interactions, and downstream defense responses. The trifluoroacetate (TFA) salt form enhances solubility and handling, facilitating its use in diverse experimental systems within plant molecular biology and immunology research.

Plant innate immunity research: Flagelin 22(TFA) is widely employed as a potent elicitor in studies of plant basal immunity. By mimicking the highly conserved flg22 epitope of bacterial flagellin, the peptide enables precise activation of pattern-triggered immunity (PTI) in a range of model species, including Arabidopsis thaliana and crop plants. Researchers use it to induce and monitor early immune responses such as reactive oxygen species (ROS) burst, mitogen-activated protein kinase (MAPK) activation, and transcriptional reprogramming, thereby elucidating the molecular architecture of plant defense signaling networks.

Receptor-ligand interaction assays: The peptide serves as a defined ligand for the FLAGELLIN-SENSING 2 (FLS2) receptor and its associated co-receptors. Its application in binding assays, co-immunoprecipitation, and surface plasmon resonance studies allows for quantitative and qualitative assessment of receptor specificity, affinity, and downstream complex formation. Such experiments are critical for characterizing receptor mutants, mapping binding domains, and screening for modulators of immune perception in plants.

Functional genomics and mutant screening: In genetic studies, Flagelin 22(TFA) provides a reliable stimulus for phenotyping plant mutants with altered immune responsiveness. By applying the peptide to mutant lines or transgenic plants, researchers can identify components involved in PTI signaling, dissect gene function, and validate genetic interactions. This approach accelerates the discovery of novel immune regulators and supports functional annotation of immunity-related genes.

Cell signaling pathway analysis: The defined sequence and high purity of the peptide enable reproducible activation of signaling pathways in cell-based assays. Application to plant cell cultures or protoplasts facilitates time-resolved analysis of phosphorylation events, secondary messenger dynamics, and transcription factor mobilization. Such studies provide mechanistic insights into early signal transduction events and inform the design of downstream functional experiments.

High-throughput screening of immune modulators: The robust and quantifiable responses elicited by Flagelin 22(TFA) make it an ideal tool for high-throughput chemical or genetic screens aimed at identifying novel modulators of plant immunity. Researchers can use the peptide to establish standardized assays for screening compound libraries, RNAi collections, or mutant populations, thereby accelerating the identification of candidates that enhance or suppress immune signaling. This application supports both fundamental research and the development of crop protection strategies through targeted manipulation of plant defense pathways.

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