Selective peptide inhibitor of c-Jun N-terminal kinase (JNK), based on residues 153-163 of JNK-interacting protein-1 (JIP-1).
CAT No: R0970
CAS No:438567-88-5
Synonyms/Alias:TI-JIP;438567-88-5;NSA56788;AKOS024456670;DA-64642;PD079064;JIP-1(153-163);S-438567-88-5;
JIP-1 (153-163) is a synthetic peptide segment derived from the c-Jun N-terminal kinase (JNK)-interacting protein 1, a scaffold protein that plays a central role in the regulation of JNK signaling pathways. As a biochemically defined peptide corresponding to amino acid residues 153 to 163 of JIP-1, it serves as a valuable molecular tool for dissecting protein-protein interactions involved in mitogen-activated protein kinase (MAPK) signaling cascades. The specific sequence and structural features of this peptide enable researchers to investigate the mechanistic basis of JNK pathway modulation, providing insights into cellular stress responses, neuronal signaling, and broader aspects of signal transduction biology.
Signal transduction research: The JIP-1 (153-163) peptide is widely utilized in studies aimed at elucidating the molecular mechanisms underlying JNK pathway regulation. By mimicking a critical segment of the scaffold protein, it allows researchers to probe the interaction interfaces between JIP-1 and its binding partners, such as kinases and downstream effectors. Incorporation of this peptide into in vitro binding assays or cell-free systems facilitates the mapping of contact sites and the identification of sequence motifs essential for complex assembly, thereby advancing understanding of how scaffold proteins orchestrate MAPK signaling specificity.
Protein-protein interaction studies: As an isolated peptide fragment, JIP-1 (153-163) serves as an effective competitive inhibitor or binding probe in experimental systems designed to characterize the dynamics of protein interactions. It can be employed to disrupt or compete with endogenous JIP-1 for binding to JNK or other associated molecules, enabling quantitative analysis of binding affinities and the delineation of interaction networks. Such studies are critical for validating interaction models and for screening small molecules or other peptides that modulate scaffold-mediated signaling.
Peptide-based assay development: The defined sequence and biochemical properties of JIP-1 (153-163) make it suitable for the development of peptide-based assays targeting JNK pathway components. It can be incorporated into fluorescence polarization, surface plasmon resonance, or enzyme-linked systems to monitor binding events in real time, providing a platform for high-throughput screening of potential modulators. These assay formats are valuable for both basic research and early-stage drug discovery efforts focused on signal transduction pathways.
Structural and biophysical analysis: The peptide is also employed in structural biology and biophysical studies aimed at elucidating the conformational determinants of JIP-1-mediated interactions. Researchers utilize JIP-1 (153-163) in nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, or circular dichroism experiments to resolve the secondary structure and binding-induced conformational changes. Such analyses contribute to a detailed understanding of scaffold protein architecture and the molecular basis of signaling complex formation.
Peptide synthesis and modification research: JIP-1 (153-163) is frequently used as a model substrate in the field of peptide chemistry, where it serves as a template for investigating synthetic strategies, sequence modifications, or labeling approaches. Its well-characterized sequence allows for the systematic evaluation of side-chain modifications, incorporation of non-natural amino acids, or conjugation with reporter groups, supporting the development of advanced peptide-based tools for biochemical and cellular studies. Through these diverse applications, JIP-1 (153-163) continues to be an indispensable resource for researchers exploring the intricacies of MAPK signaling and peptide functionalization.
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