MUC1, mucin core is a glycoprotein-derived peptide rich in serine, threonine, and proline residues that influence extended and helical structures. Researchers examine its role in glycosylation patterns, solvent-dependent conformations, and protein-epitope interactions. The sequence supports structural mapping of mucin-like regions. Its flexibility enables detailed biophysical studies.
CAT No: R2413
CAS No:149205-73-2
Synonyms/Alias:MUC1, mucin core;149205-73-2;APDTRPAPG;AKOS040756856;DA-55759;G13485;Gly1-Val2-Thr3-Ser4-Ala5-Pro6-Asp7-Thr8-Arg9-Pro10-Ala11-Pro12-Gly13-Ser14-Thr15-Ala16;
MUC1, mucin core, is a high molecular weight glycoprotein that is abundantly expressed on the apical surface of epithelial cells in various tissues, such as the respiratory tract, gastrointestinal tract, and mammary glands. Characterized by its extensive glycosylation and unique tandem repeat domains, MUC1 plays a crucial role in forming protective mucous barriers and mediating cell signaling events. Its structural complexity, featuring a heavily O-glycosylated extracellular domain, allows for dynamic interactions with the cellular microenvironment, impacting cellular adhesion, immune response modulation, and pathogen defense. Due to these multifunctional properties, the mucin core of MUC1 is a valuable research tool for a wide spectrum of scientific disciplines, including glycobiology, oncology, immunology, and cell biology.
Cancer Biology Research: In cancer biology, MUC1 serves as a prominent model for studying tumor-associated glycoproteins, given its altered expression and glycosylation patterns in many epithelial cancers. Researchers utilize this glycoprotein to investigate mechanisms of tumor progression, metastasis, and cellular transformation. Its aberrant localization and modification in malignant cells make it a key target for exploring tumor-host interactions, immune evasion strategies, and the development of diagnostic biomarkers. By examining how MUC1 contributes to the tumor microenvironment, scientists gain insights into cancer cell signaling pathways, cellular adhesion, and the disruption of normal tissue architecture.
Glycobiology and Structural Analysis: The mucin core of MUC1 is extensively employed in glycobiology studies aimed at elucidating the structure-function relationships of mucin-type O-glycans. Researchers leverage its well-defined tandem repeat regions to analyze glycosylation patterns, enzymatic modifications, and the biosynthetic pathways of mucin-type oligosaccharides. These investigations provide a deeper understanding of how glycan structures influence protein stability, cellular recognition, and intercellular communication. Additionally, the mucin core serves as a reference substrate for developing and validating analytical techniques, such as mass spectrometry and glycan microarrays, which are essential for characterizing complex carbohydrate structures.
Immunological Studies: MUC1 is a valuable tool in immunology research, particularly in the study of mucosal immunity and immune tolerance. Its extracellular domain, rich in carbohydrate moieties, interacts with various immune cell receptors, influencing immune surveillance and the modulation of inflammatory responses. Scientists use it to dissect the mechanisms by which mucins regulate immune cell trafficking, antigen presentation, and the establishment of immune barriers at epithelial surfaces. Furthermore, research involving MUC1 provides insight into how changes in glycosylation affect immune recognition and the potential for immune escape in pathological conditions.
Microbial Pathogenesis: The mucin core of MUC1 is frequently utilized in studies investigating host-pathogen interactions, especially in the context of mucosal surfaces. Its dense glycan shield acts as a decoy for microbial adhesins, thereby preventing pathogen attachment and colonization. Researchers employ MUC1 constructs to model the first line of defense against bacteria, viruses, and other pathogens, unraveling the molecular mechanisms by which mucins modulate microbial binding and clearance. These findings contribute to the broader understanding of innate immunity and the development of strategies to enhance mucosal protection.
Biomaterials and Surface Engineering: In the field of biomaterials, MUC1-derived glycoproteins are explored for their anti-adhesive and lubricating properties. Scientists incorporate mucin core fragments into the design of bioinspired coatings and hydrogels to mimic the protective functions of natural mucous layers. These applications aim to reduce biofouling, improve biocompatibility, and create surfaces resistant to microbial colonization. By harnessing the unique physicochemical attributes of MUC1, researchers advance the development of next-generation materials for use in biotechnology, medical devices, and tissue engineering.
Cell Adhesion and Signaling: Beyond its protective and structural roles, MUC1 is integral to the study of cell adhesion and intracellular signaling. Its cytoplasmic tail is involved in transmitting signals from the extracellular environment to the cell interior, influencing processes such as proliferation, differentiation, and apoptosis. Researchers investigate how the mucin core modulates cell-cell and cell-matrix interactions, thereby impacting tissue organization and response to external stimuli. These studies are pivotal for unraveling the complex crosstalk between epithelial cells and their surroundings, contributing to advancements in regenerative medicine and the understanding of tissue homeostasis.
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