Jagged-1 (188-204) is a fragment of the Jagged-1 (JAG-1) protein. JAG-1 is a Notch ligand highly expressed in cultured and primary multiple myeloma (MM) cells. JAG-1 induces maturation of monocyte-derived human dendritic cells.
CAT No: R1461
CAS No:219127-21-6
Synonyms/Alias:219127-21-6;Jagged-1 pound 188-204 pound(c);Jagged-1 (188-204);Jagged-1 ??188-204??;AKOS040764033;H-Cys-Asp-Asp-Tyr-Tyr-Tyr-Gly-Phe-Gly-Cys-Asn-Lys-Phe-Cys-Arg-Pro-Arg-OH;
Jagged-1 188-204 is a synthetic peptide fragment derived from the extracellular domain of the human Jagged-1 protein, a well-characterized ligand in the Notch signaling pathway. This peptide encompasses amino acids 188 to 204, a region implicated in mediating protein-protein interactions critical for cell fate determination and developmental signaling. As a tool compound, it is widely utilized in studies probing the molecular mechanisms of Notch receptor activation, intercellular communication, and the modulation of downstream transcriptional events. Its defined sequence and biochemical specificity make it an invaluable asset for dissecting the multifaceted roles of Jagged-1 in cellular signaling networks.
Signal transduction research: The 188-204 fragment of Jagged-1 serves as a targeted probe for investigating the molecular underpinnings of Notch signaling. By mimicking a biologically relevant region of the native ligand, it enables researchers to study ligand-receptor interactions in a controlled environment. Experimental systems employing this peptide allow for the selective activation or inhibition of Notch receptors, facilitating the elucidation of downstream signaling cascades and their impact on gene expression, differentiation, and cellular communication.
Protein-protein interaction studies: As an epitope within the functional domain of Jagged-1, this peptide is frequently employed in assays designed to map binding interfaces between Jagged-1 and its cognate Notch receptors or associated co-factors. Surface plasmon resonance, co-immunoprecipitation, and pull-down experiments utilize the 188-204 sequence to quantify binding affinities, characterize interaction kinetics, and identify critical residues responsible for ligand recognition. These insights are essential for understanding the structural determinants governing Notch pathway specificity.
Peptide-based inhibitor screening: The defined sequence of Jagged-1 188-204 provides a template for the rational design and screening of small-molecule or peptide-based inhibitors targeting the Notch pathway. By serving as a competitive substrate or decoy ligand, it enables the identification of compounds capable of modulating ligand-receptor engagement. Such applications are instrumental in the development of research tools aimed at dissecting the regulatory checkpoints within the Notch signaling axis and evaluating potential modulators in preclinical models.
Antibody generation and epitope mapping: The peptide fragment corresponding to residues 188-204 of Jagged-1 is commonly used as an immunogen for the production of sequence-specific antibodies. These antibodies are valuable reagents for detecting endogenous Jagged-1 in immunoassays, Western blotting, or immunohistochemical applications. Furthermore, the peptide assists in fine-mapping antibody epitopes, enabling the characterization of antibody specificity and cross-reactivity, which is essential for the validation of immunological reagents in basic and applied research.
Biochemical assay development: Incorporation of the Jagged-1 188-204 peptide into in vitro assay platforms enhances the specificity and reproducibility of biochemical measurements related to Notch pathway activity. It can be immobilized on solid supports for use in ELISA formats, affinity purification, or high-throughput screening assays. The controlled presentation of this peptide sequence allows for the quantitative assessment of ligand-receptor interactions, the evaluation of pathway modulators, and the standardization of experimental conditions across diverse research applications.
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