ADP-ribosylation factor GTPase-activating protein 3 (152-160)

ADP-ribosylation factor GTPase-activating protein 3 (152-160) is a synthetic peptide fragment corresponding to amino acids 152 through 160 of the ARF GAP3 protein. As a specialized peptide reagent, it represents a critical tool for researchers investigating the regulatory mechanisms of small GTPases, particularly those involved in vesicular trafficking, cytoskeletal dynamics, and signal transduction. The sequence is derived from a functionally significant region of ARF GAP3, a protein that modulates the activity of ADP-ribosylation factors by stimulating their intrinsic GTPase activity, thus facilitating the transition from the active GTP-bound state to the inactive GDP-bound form. This peptide serves as a valuable molecular probe for dissecting protein-protein interactions, mapping functional domains, and studying post-translational regulation within the ARF family signaling pathways.

Protein-protein interaction mapping: The peptide fragment is widely employed in the characterization of binding interfaces between ARF GAP3 and its target proteins or regulatory partners. By serving as a defined epitope, it enables affinity-based assays such as peptide pull-downs, surface plasmon resonance, or co-immunoprecipitation studies, thereby facilitating the identification of specific interactors and the delineation of structural motifs essential for functional association. Its use helps clarify how ARF GAP3 recognizes and modulates ARF GTPases or other accessory proteins involved in vesicular trafficking.

Signal transduction research: Within the context of cell signaling, the ARF GAP3 (152-160) peptide is instrumental for dissecting the mechanistic details of GTPase cycling and downstream signaling events. Researchers utilize it to competitively inhibit or mimic endogenous sequences, allowing the investigation of pathway modulation, regulatory feedback mechanisms, and the consequences of altered ARF GAP3 activity. Such studies are crucial for understanding the dynamic regulation of membrane trafficking and actin cytoskeleton remodeling in diverse cellular processes.

Antibody production and epitope mapping: As a synthetic peptide corresponding to a unique region of ARF GAP3, this fragment is frequently used as an immunogen for generating sequence-specific antibodies. These antibodies are invaluable for detecting and quantifying ARF GAP3 expression in various experimental systems, including Western blotting, immunoprecipitation, and immunofluorescence applications. Additionally, the peptide serves as a reference standard in epitope mapping experiments, aiding in the validation and characterization of antibody specificity.

Peptide-based assay development: The defined sequence of ARF GAP3 (152-160) supports the creation of sensitive and selective assays to monitor enzymatic activity, binding kinetics, or post-translational modifications. Incorporation of this peptide into in vitro assay platforms enables the quantitative analysis of GAP activity, substrate specificity, or the effects of small molecule modulators. Such assays are essential for high-throughput screening efforts and for elucidating the molecular pharmacology of ARF signaling regulators.

Structural and functional domain analysis: Researchers often employ this peptide fragment to interrogate the structural features and functional domains of ARF GAP3. Through techniques such as nuclear magnetic resonance (NMR), circular dichroism spectroscopy, or crystallography, the peptide can reveal secondary structure propensities, conformational dynamics, or key residues involved in molecular recognition. These studies contribute to a detailed understanding of the sequence-structure-function relationships governing ARF GAP3 activity and its role in cellular homeostasis.

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