Recombinant Human MUC5AC protein

Mucin 5AC (MUC5AC) is a high-molecular-weight glycoprotein belonging to the gel-forming mucin family, primarily secreted by goblet cells in mucosal tissues of the respiratory, gastrointestinal, and reproductive tracts. It plays a critical role in forming the viscoelastic mucus layer that protects epithelial surfaces from pathogens, particulate matter, and chemical irritants. Structurally, MUC5AC contains cysteine-rich domains at its N- and C-termini, which facilitate polymerization via disulfide bonds, and a central tandem repeat region heavily modified by O-glycosylation. These post-translational modifications contribute to its gel-like properties and resistance to proteolytic degradation.

Dysregulation of MUC5AC is implicated in multiple pathologies. Overproduction is associated with chronic respiratory diseases like asthma, chronic obstructive pulmonary disease (COPD), and cystic fibrosis, where excessive mucus obstructs airways. Conversely, reduced expression may compromise mucosal defense, increasing susceptibility to infections. Studying MUC5AC's role in these conditions requires well-characterized recombinant proteins, which are produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper glycosylation and folding.

Recombinant MUC5AC proteins enable researchers to investigate mucus biophysics, host-pathogen interactions, and signaling pathways regulating mucin secretion. They serve as standards in diagnostic assays, tools for drug screening (e.g., mucolytic agents), and substrates for developing mucoadhesive drug delivery systems. Recent advances also explore their potential as biomarkers or therapeutic targets. However, challenges remain in replicating native glycan patterns and multimerization states, which are critical for functional studies. Ongoing research aims to optimize production methods and elucidate structure-function relationships to advance therapeutic strategies for mucin-related disorders.