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 the human Annexin A1 protein, specifically comprising amino acids 1 through 25 in a dephosphorylated state. This peptide is widely recognized for its ability to mimic the bioactive domain of Annexin A1, a protein involved in various cellular processes such as membrane trafficking, inflammation modulation, and cell signaling. The dephosphorylated form of this peptide is particularly valuable for research focused on phosphorylation-dependent mechanisms, offering a precise tool for dissecting the functional consequences of post-translational modifications. Its structure allows for high specificity in experimental systems, making it an essential reagent in studies seeking to elucidate the molecular pathways regulated by Annexin A1 and its derivatives.
Inflammation Research: In the field of inflammation research, Annexin A1 (1-25) (dephosphorylated) serves as a critical probe for exploring the anti-inflammatory actions of Annexin A1. By utilizing this peptide in in vitro cell culture models or ex vivo tissue assays, researchers can investigate how the dephosphorylated N-terminal fragment modulates leukocyte migration, cytokine release, and the resolution phase of inflammation. The absence of phosphorylation in this peptide enables the differentiation of phosphorylation-dependent and independent signaling pathways, providing nuanced insights into the regulatory mechanisms that control inflammatory responses. This application is particularly relevant for studies aiming to identify novel therapeutic targets or understand the molecular basis of chronic inflammatory diseases.
Cell Signaling Pathways: The dephosphorylated Annexin A1 (1-25) fragment is frequently employed to dissect cell signaling cascades, particularly those involving the glucocorticoid-induced annexin pathway. By introducing this peptide into cellular systems, scientists can observe its influence on the activation or inhibition of downstream effectors, such as phospholipase A2 or MAP kinases. The peptide's ability to interact with specific cellular receptors or signaling molecules makes it a valuable tool for mapping the intricate networks that govern cell growth, differentiation, and apoptosis. Its use extends to the analysis of cross-talk between signaling pathways, thereby advancing our understanding of cellular homeostasis and stress responses.
Membrane Biology Studies: Researchers investigating membrane dynamics and vesicle trafficking often utilize Annexin A1 (1-25) (dephosphorylated) to probe the role of Annexin A1 in membrane fusion, curvature, and repair. The peptide's unique structural properties facilitate its interaction with phospholipid membranes, enabling detailed studies of membrane-associated events in live cells or model membrane systems. By observing the effects of the dephosphorylated peptide on endocytosis, exocytosis, and membrane resealing, scientists can unravel the molecular mechanisms underpinning cellular membrane integrity and communication.
Protein-Protein Interaction Analysis: Annexin A1 (1-25) (dephosphorylated) is also instrumental in characterizing protein-protein interactions, particularly those involving the Annexin family or signaling proteins implicated in inflammation and cell motility. Through techniques such as pull-down assays, surface plasmon resonance, or co-immunoprecipitation, the peptide can be used to identify binding partners and define interaction domains. This application is vital for constructing detailed interaction maps that inform drug discovery efforts and the development of peptide-based modulators.
Drug Discovery and Screening: In the context of drug discovery, the dephosphorylated N-terminal fragment of Annexin A1 is utilized as a reference ligand or functional probe in high-throughput screening assays. Its incorporation into assay platforms allows for the identification of small molecules or biologics that modulate Annexin A1-related pathways, facilitating the early stages of therapeutic development. By providing a reliable and biologically relevant target, the peptide streamlines the screening process and enhances the translational potential of candidate compounds. Collectively, these diverse applications underscore the scientific value of Annexin A1 (1-25) (dephosphorylated) (human) in advancing fundamental and translational research across multiple disciplines.
2. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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