Ac2-26 is Annexin A1 (AnxA1) N-terminal-derived peptide, and acts as inhibitor of leukocyte extravasation. It can reduce neutrophil adhesion and emigration, promote detachment of neutrophils from activated mesenteric endothelium and accelerate epithelial wound repair after induced colonic injury in mice in vivo. It shows anti-inflammatory effect.
CAT No: 10-101-239
CAS No:151988-33-9
Synonyms/Alias:Ac2-26;151988-33-9;Ac2-26 (human) (ammonium salt);Annexin-1 (2-26) (human);AnxA1 mimetic peptide;Lipocortin-1 (2-26);AKOS024456812;FA108920;Annexin A1(1-25)(dephosphorylated)(human)ammonium salt;
Annexin A1 (1-25) (dephosphorylated) (human) is a synthetic peptide fragment derived from the N-terminal region of human Annexin A1, specifically encompassing amino acids 1 to 25 in its dephosphorylated form. As a member of the annexin family, Annexin A1 is recognized for its calcium-dependent phospholipid-binding properties and its pivotal role in modulating cellular processes such as membrane trafficking, inflammation, and cell signaling. The dephosphorylated state of this peptide segment provides a unique tool for dissecting phosphorylation-dependent regulatory mechanisms, allowing researchers to investigate the functional consequences of post-translational modifications on Annexin A1-mediated pathways. Its structural and functional attributes make it a valuable reagent for studies focused on peptide-protein interactions, signal transduction, and the biochemical underpinnings of inflammation and cell migration.
Peptide signaling research: The dephosphorylated Annexin A1 (1-25) fragment serves as a powerful probe for studying the molecular mechanisms underlying peptide-mediated cell signaling. By mimicking the endogenous N-terminal region of Annexin A1, this peptide enables researchers to explore how specific phosphorylation states influence the activation or inhibition of downstream signaling cascades. Its defined sequence and lack of phosphorylation allow for controlled experimental conditions when characterizing the interactions between Annexin A1 and its cellular binding partners, such as formyl peptide receptors and other signaling molecules involved in immune cell regulation.
Inflammatory pathway analysis: In the context of inflammation research, the use of the Annexin A1 (1-25) (dephosphorylated) peptide facilitates detailed examination of the anti-inflammatory actions attributed to Annexin A1. Investigators can employ this fragment to delineate the precise molecular events by which Annexin A1 modulates leukocyte migration, cytokine release, and resolution of inflammatory responses. By comparing the effects of phosphorylated versus dephosphorylated peptide forms, it becomes possible to dissect the contribution of post-translational regulation to the peptide's biological activity in inflammation-related models.
Protein-protein interaction studies: The defined 1-25 amino acid sequence of this peptide is particularly suited for in vitro assays aimed at mapping interaction domains between Annexin A1 and its effector proteins. Surface plasmon resonance, pull-down, and co-immunoprecipitation assays can utilize the dephosphorylated peptide to identify and characterize binding affinities, kinetic parameters, and the structural basis of complex formation. Such studies are instrumental in advancing the understanding of how Annexin A1 orchestrates cellular responses through direct protein interactions.
Peptide structure-function analysis: Structural biologists and biochemists can leverage the Annexin A1 (1-25) (dephosphorylated) peptide to investigate the relationship between primary sequence, post-translational modification, and functional output. The availability of a well-defined dephosphorylated fragment allows for comparative analyses using biophysical techniques such as NMR spectroscopy, circular dichroism, or crystallography. Insights gained from these studies contribute to a deeper comprehension of how phosphorylation modulates peptide conformation and its downstream effects on cellular processes.
Cell migration and cytoskeletal dynamics: Researchers interested in cell motility and cytoskeletal rearrangement can employ this peptide fragment to probe the involvement of Annexin A1 in regulating actin dynamics and membrane-cytoskeleton interactions. The dephosphorylated form offers a means to assess the specific influence of phosphorylation status on Annexin A1's capacity to coordinate cytoskeletal reorganization, cell adhesion, and migration in various experimental systems, including wound healing assays and live-cell imaging platforms.
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