Ac2-26 TFA, an active N-terminal peptide of annexin A1 (AnxA1), attenuates ischemia-reperfusion-induced acute lung injury. Ac2-26 also decreases AnxA1 protein expression, inhibits the activation of NF-κB and MAPK pathways in the injured lung tissue.
CAT No: R1145
Ac2-26 TFA, a synthetic peptide corresponding to the N-terminal 25 amino acids of Annexin A1 (AnxA1), is widely recognized for its role as a functional fragment that mimics the bioactive region of the parent protein. As a research-use peptide, it is typically supplied as the trifluoroacetate (TFA) salt to enhance stability and solubility. Ac2-26 is of significant interest in the study of cell signaling, inflammation, and membrane biology due to its ability to engage with specific cellular receptors and modulate intracellular pathways. Its well-characterized sequence and biochemical properties make it a valuable tool for dissecting the mechanistic underpinnings of Annexin A1-mediated processes in diverse experimental systems.
Peptide signaling pathway investigation: Researchers employ Ac2-26 TFA to probe the mechanisms of Annexin A1-derived peptide signaling in cellular models. By engaging formyl peptide receptors (FPRs), the peptide enables detailed examination of downstream signaling cascades, such as modulation of phospholipase A2 activity, calcium mobilization, and MAP kinase pathways. This application is central to understanding how specific peptide domains influence receptor-mediated cellular responses, providing insights into the broader field of peptide-receptor interactions.
Inflammation and immune response studies: The AnxA1-derived sequence of Ac2-26 is instrumental in exploring the molecular basis of inflammatory regulation. In vitro models utilizing this peptide allow investigators to assess its impact on leukocyte migration, cytokine release, and the resolution phase of inflammation. These studies help clarify the anti-inflammatory potential and immunomodulatory functions of Annexin A1 fragments, supporting advances in the understanding of innate immune mechanisms.
Cellular membrane interaction analysis: Ac2-26 TFA is frequently used to study peptide-lipid interactions and membrane dynamics. Its amphipathic nature and affinity for phospholipid bilayers make it a valuable probe for characterizing the biophysical properties of cell membranes. Researchers can utilize this peptide to elucidate how Annexin A1 domains contribute to membrane binding, curvature induction, and vesicular trafficking, which are critical factors in cellular homeostasis and signaling.
Peptide structure-function relationship research: The defined amino acid sequence of Ac2-26 provides an excellent model for investigating the structural determinants of peptide function. Through mutational analysis, biophysical characterization, and structure-activity relationship studies, scientists can dissect the contributions of specific residues to receptor binding, biological activity, and stability. These insights inform the rational design of peptide analogs and contribute to the broader understanding of protein domain functionality.
Peptide-based assay development: Owing to its well-characterized activity and receptor specificity, Ac2-26 TFA is utilized in the development and validation of peptide-based bioassays. These assays are essential for screening modulators of Annexin A1 pathways, evaluating receptor-ligand interactions, and quantifying peptide activity in complex biological samples. The use of this synthetic fragment supports the creation of robust, reproducible platforms for high-throughput biochemical and pharmacological studies.
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