ETV6-AML1 fusion protein
ETV6-AML1 fusion protein (332-346) is a synthetic peptide corresponding to a specific region of the fusion junction between the ETV6 (TEL) and AML1 (RUNX1) transcription factors, which are frequently involved in chromosomal translocations observed in certain hematological malignancies, particularly childhood acute lymphoblastic leukemia (ALL). As a peptide fragment derived from the fusion interface, it serves as a valuable molecular tool for dissecting the structural and functional implications of the ETV6-AML1 oncogenic fusion, offering researchers a targeted approach to study the altered protein-protein interactions and downstream signaling events that arise from this genetic rearrangement. Its well-defined sequence and biochemical properties make it suitable for applications in molecular biology, cancer research, and peptide-based assay development.
Protein-protein interaction studies: The ETV6-AML1 fusion region peptide is commonly used to investigate the molecular interactions that occur at the fusion junction, which is critical for understanding how the chimeric protein alters normal cellular function. By serving as a binding substrate or competitor in in vitro assays, the peptide enables researchers to map interaction domains, characterize binding affinities, and identify novel partners that may contribute to leukemogenesis. Such studies are essential for elucidating the mechanistic basis of aberrant transcriptional regulation mediated by the fusion protein.
Antibody generation and validation: As a highly specific epitope representative of the fusion breakpoint, the peptide is frequently employed as an immunogen for the development of monoclonal and polyclonal antibodies that recognize the unique ETV6-AML1 junction. These antibodies are indispensable for the sensitive detection of the fusion protein in cell lysates, tissue samples, or immunoassays, facilitating both basic research and diagnostic method development. Additionally, the peptide is valuable for validating antibody specificity in western blotting, ELISA, and immunoprecipitation applications.
Leukemia biomarker research: The unique sequence of this fusion junction peptide makes it a powerful tool for developing and optimizing peptide-based assays aimed at detecting the presence of ETV6-AML1 fusion events in biological samples. By serving as a standard or calibrator in mass spectrometry or immunoassays, it aids researchers in quantifying minimal residual disease, tracking disease progression, or evaluating the molecular response to experimental interventions in preclinical research models of leukemia.
Peptide structure-function analysis: The defined sequence of the ETV6-AML1 fusion protein (332-346) peptide allows for detailed biophysical and structural studies, such as circular dichroism spectroscopy, NMR, or molecular modeling, to assess conformational properties and stability. Insights gained from such analyses inform the understanding of how the fusion region contributes to altered protein folding, stability, or interactions, thereby advancing knowledge of oncogenic protein mechanisms at the molecular level.
Peptide-based assay development: The synthetic peptide is highly suitable for use as a reference standard, positive control, or assay substrate in a variety of biochemical and cell-free assay systems. Its reproducibility and specificity enable the development of robust, quantitative methods for investigating the activity, inhibition, or modification of the fusion protein, supporting high-throughput screening and mechanistic studies in leukemia research. By integrating this peptide into assay platforms, researchers can achieve greater accuracy and consistency in experimental workflows focused on ETV6-AML1 fusion biology.
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