Mucin-1 precursor (12-20)

Mucin-1 precursor (12-20) is a synthetic peptide fragment derived from the N-terminal region of the MUC1 glycoprotein, specifically encompassing amino acid residues 12 to 20. As a segment of the larger MUC1 protein, which is heavily glycosylated and expressed on the apical surface of many epithelial tissues, this peptide is of significant interest in biochemical and molecular research focused on cell surface interactions, glycoprotein function, and cancer biology. The defined sequence of the Mucin-1 precursor (12-20) peptide allows researchers to investigate the structural and functional attributes of the MUC1 protein in a controlled and reproducible manner, making it a valuable tool for probing peptide-mediated cellular processes and for developing targeted analytical assays.

Epitope mapping: The 12-20 region of the MUC1 precursor is frequently utilized in epitope mapping studies to identify and characterize antibody binding sites within the MUC1 protein. By employing this peptide fragment, researchers can delineate the specific amino acid residues recognized by monoclonal or polyclonal antibodies, facilitating the development of highly specific immunodetection reagents. Such mapping is critical for advancing the understanding of immune recognition of MUC1 in both normal and pathological contexts, including cancer immunology and biomarker research.

Peptide-based assay development: The defined structure of this peptide supports its use as a standard or reference in the development and calibration of peptide-based analytical assays, such as enzyme-linked immunosorbent assays (ELISA) and surface plasmon resonance (SPR) assays. Incorporation of the Mucin-1 precursor (12-20) sequence enables precise quantification and detection of MUC1-related epitopes, aiding in the validation of assay performance and the establishment of reliable diagnostic or research protocols.

Protein-protein interaction studies: As a representative fragment of the MUC1 extracellular domain, this peptide is employed in in vitro studies to investigate interactions between MUC1 and other proteins, such as lectins, adhesion molecules, or signaling partners. By isolating the 12-20 region, researchers can dissect the molecular determinants that govern MUC1-mediated cell adhesion, signaling cascades, or modulation of the tumor microenvironment, thereby contributing to a more nuanced understanding of glycoprotein biology.

Peptide modification and conjugation research: The Mucin-1 precursor (12-20) peptide serves as a versatile scaffold for chemical modification, conjugation, or labeling studies. Its defined sequence and accessible functional groups make it suitable for attachment to fluorophores, biotin, or carrier proteins, enabling the creation of custom probes or affinity reagents. Such modifications are instrumental in designing advanced imaging tools, affinity purification systems, or targeted delivery vehicles for research applications.

Immunogenicity and vaccine research: The 12-20 peptide fragment is often investigated for its immunogenic properties in preclinical research settings, particularly in the context of synthetic vaccine design or immune response profiling. By assessing the ability of this peptide to elicit specific T-cell or B-cell responses in vitro, scientists can gain insights into the immunological features of MUC1-derived epitopes, supporting the rational design of immunotherapeutic strategies and the evaluation of immune recognition mechanisms in disease models.

1. Quantitative Analysis of Ligands Effects on Bioefficacy of Nanoemulsion encapsulating Depigmenting Active

2. The spatiotemporal control of signalling and trafficking of the GLP-1R

3. Immune responses to peptides containing homocitrulline or citrulline in the DR4-transgenic mouse model of rheumatoid arthritis

4. Zeta-potential-changing nanoparticles conjugated with cell-penetrating peptides for enhanced transfection efficiency

5. Multifunctional peptide-oligonucleotide conjugate promoted sensitive electrochemical biosensing of cardiac troponin I