MUC5AC, Analog 1

Product Name: MUC5AC, Analog 1

Sequence One Letter Code: GTTPSPVPTTSTTSAP

Sequence Three Letter Code: H-Gly-Thr-Thr-Pro-Ser-Pro-Val-Pro-Thr- Thr-Ser-Thr-Thr-Ser-Ala-Pro-OH

Chemical Formula:C63H104N16O26

Molecular Weight: 1501.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: MUC5AC Analog 1 is a synthetic peptide derived from the tandem repeat domain of the human mucin MUC5AC, specifically reflecting the conserved TTSTTSAP motif. MUC5AC is a major gel-forming mucin expressed predominantly in gastric and tracheobronchial epithelium, where it contributes to mucosal barrier protection and lubrication. Aberrant expression and glycosylation of MUC5AC have been implicated in inflammatory airway diseases and multiple epithelial cancers. This analog represents a consensus repeat sequence commonly used to investigate mucin structure, glycosylation patterns, and antigenic determinants. Peptides derived from this region facilitate studies of tumor-associated mucin expression, antibody recognition, and epithelial immune interactions. They also support research into mucin polymerization and mucosal defense mechanisms. MUC5AC Analog 1 is therefore a useful molecular tool in epithelial biology, cancer research, and investigations of mucin-mediated host–pathogen interactions.

Current Research: MUC5AC Analog 1 has become an important molecular tool for dissecting the structural and functional properties of gel-forming mucins in both physiological and pathological contexts. Derived from the conserved TTSTTSAP tandem repeat motif of human MUC5AC, this peptide models a core sequence within the heavily O-glycosylated central domain of the native protein. Recent research has focused on how repeat-region architecture and glycosylation density influence mucin polymerization, viscoelastic properties, and barrier integrity in gastric and airway epithelia. In respiratory biology, altered MUC5AC expression is strongly associated with asthma, chronic obstructive pulmonary disease (COPD), and viral-induced airway remodeling. Studies using repeat-derived peptides help define how inflammatory cytokines such as IL-13 regulate mucin overproduction and modify glycosyltransferase activity, thereby reshaping glycan composition. Because aberrant glycosylation creates tumor-associated carbohydrate antigens, MUC5AC repeat peptides are widely applied in cancer research to map epitope accessibility, antibody specificity, and immune recognition patterns in gastric, pancreatic, and colorectal malignancies. Structural investigations also employ repeat analogs to evaluate interactions between mucins and microbial adhesins. Pathogens such as Helicobacter pylori and respiratory bacteria exploit mucin glycans for colonization; defined repeat motifs facilitate controlled studies of host–pathogen binding dynamics. In addition, synthetic repeat peptides support mass spectrometry–based glycoproteomics workflows aimed at characterizing site-specific O-glycosylation. Emerging work in tumor immunology further highlights MUC5AC-derived sequences as potential immunogenic targets. Vaccination strategies and monoclonal antibody development programs use repeat-region peptides to generate immune responses against tumor-associated mucin variants. These approaches aim to selectively target aberrantly glycosylated mucins without disrupting normal epithelial protection. Collectively, MUC5AC Analog 1 provides a reductionist yet biologically relevant platform for investigating mucin biochemistry, glycan-mediated signaling, epithelial barrier regulation, and oncogenic transformation. Its defined sequence enables reproducible mechanistic studies across epithelial biology, airway inflammation, and mucin-driven tumor progression research.