ETV6-AML1 fusion protein
ETV6-AML1 fusion protein (334-342) is a synthetic peptide fragment derived from the junctional region of the ETV6 (TEL) and AML1 (RUNX1) genes, which are commonly fused as a result of the t(12;21)(p13;q22) chromosomal translocation in certain leukemias. This peptide represents a specific sequence within the fusion protein that is of significant interest in the study of oncogenic mechanisms, protein-protein interactions, and molecular diagnostics in hematological malignancies. Its unique sequence and biochemical properties enable researchers to investigate the structural and functional consequences of the ETV6-AML1 fusion and its role in leukemogenesis, as well as to develop tools for the detection and characterization of this oncogenic event.
Fusion protein research: The ETV6-AML1 (334-342) peptide serves as a valuable model for studying the molecular features of the ETV6-AML1 fusion protein, a critical driver in pediatric acute lymphoblastic leukemia (ALL). By providing a defined fragment from the fusion junction, this peptide enables detailed analyses of the structural changes and altered protein domains resulting from the translocation. Researchers can use it to elucidate the impact of the fusion on DNA binding, transcriptional regulation, and the disruption of normal hematopoietic differentiation pathways.
Antibody development: The defined epitope represented by this peptide fragment is highly useful in the generation and validation of antibodies specific to the ETV6-AML1 fusion junction. Such antibodies are essential for immunoassays, including Western blotting, ELISA, and immunoprecipitation, which require high specificity to distinguish the fusion protein from endogenous ETV6 and AML1 proteins. Employing this peptide as an immunogen or as a reference standard supports the creation of robust detection reagents for research and diagnostic purposes.
Peptide-based assay development: The synthetic ETV6-AML1 (334-342) sequence provides a reliable substrate for designing and optimizing peptide-based assays aimed at detecting the presence of the fusion protein in biological samples. These assays are integral to molecular diagnostics and minimal residual disease (MRD) monitoring in leukemia research, as they facilitate the sensitive and specific identification of the fusion event at the protein level. The use of this peptide aids in assay calibration, method validation, and the establishment of quantitative detection protocols.
Protein-protein interaction studies: The ETV6-AML1 fusion region is implicated in aberrant interactions with other nuclear proteins and transcriptional regulators. Incorporating the (334-342) peptide into binding assays, pull-down experiments, or surface plasmon resonance studies allows researchers to map interaction interfaces and assess the affinity and specificity of binding partners. These studies contribute to a deeper understanding of the oncogenic signaling networks perturbed by the fusion and may inform the identification of novel therapeutic targets.
Epitope mapping and structural biology: The defined amino acid sequence of the ETV6-AML1 (334-342) peptide is instrumental in mapping linear epitopes recognized by antibodies or T-cell receptors. It can be used in epitope scanning arrays or crystallographic studies to characterize the antigenic landscape of the fusion protein. Such applications are critical for dissecting immune recognition, refining antibody specificity, and advancing structural insights into the fusion junction, thereby supporting the development of next-generation research tools in leukemia biology.
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