BCR/ABL 210 kD fusion protein (21-29)

BCR/ABL 210 kD fusion protein (21-29) is a synthetic peptide fragment corresponding to amino acids 21 through 29 of the BCR/ABL fusion protein, a hallmark molecular abnormality resulting from the Philadelphia chromosome translocation commonly observed in chronic myeloid leukemia (CML) and some acute lymphoblastic leukemias. This peptide segment represents a key region within the fusion junction, making it highly relevant for studies focused on the molecular mechanisms underlying aberrant tyrosine kinase activity, oncogenic signaling, and protein-protein interactions associated with leukemogenesis. Its well-defined sequence and biochemical properties render it a valuable tool for researchers investigating the structural and functional consequences of the BCR/ABL fusion event.

Signal transduction research: The peptide is widely utilized in studies aiming to dissect the signaling pathways activated by the BCR/ABL fusion protein. By mimicking a critical region of the chimeric kinase, it serves as a substrate or competitive inhibitor in kinase assays, enabling the assessment of phosphorylation dynamics, substrate specificity, and downstream effector recruitment. This application is instrumental in elucidating how the fusion protein alters normal cellular signaling, contributing to uncontrolled proliferation and survival of hematopoietic cells.

Antibody development and validation: The defined sequence of this peptide fragment is frequently employed as an immunogen or as a specificity control in the generation and validation of monoclonal or polyclonal antibodies targeting the BCR/ABL fusion region. By providing a precise epitope, it aids in the production of high-affinity, sequence-specific antibodies for use in Western blotting, immunoprecipitation, or immunohistochemistry. Such antibodies are essential for the sensitive detection and quantification of the BCR/ABL fusion protein in various experimental systems.

Peptide-based assay development: The BCR/ABL 210 kD fusion protein (21-29) peptide is an ideal standard for the development and optimization of peptide-based assays, including enzyme-linked immunosorbent assays (ELISA) and mass spectrometry-based detection methods. Its unique sequence allows for the establishment of assays that specifically measure the presence or activity of the fusion protein or its interacting partners, facilitating both basic research and high-throughput screening applications.

Protein interaction studies: Researchers leverage this peptide to investigate molecular interactions between the BCR/ABL fusion protein and its cellular binding partners. By incorporating the peptide into pulldown or binding assays, it is possible to map interaction domains, assess binding affinities, and identify novel regulatory proteins that associate with the fusion region. These studies provide critical insights into the molecular networks perturbed by the oncogenic kinase and may reveal potential targets for therapeutic intervention.

Cellular model system calibration: The synthetic peptide is also valuable for calibrating cellular models engineered to express the BCR/ABL fusion protein. By serving as a reference standard or spike-in control, it ensures the accuracy and reproducibility of quantitative assays measuring fusion protein expression, post-translational modifications, or functional activity within cell lysates. Such calibration is particularly important for comparative studies, high-content screening, and the validation of genetic or pharmacological perturbations in BCR/ABL-driven systems.

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