Recombinant GSDMC protein (His tag)

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Recombinant Human Gasdermin-C (GSDMC) Fragment (residues 315-508) is a high-purity protein designed for structural and biochemical studies. This 194-amino acid fragment represents a stable, soluble region of the full-length protein, which plays a critical role in mediating pyroptosis—a form of inflammatory cell death—through its pore-forming activity upon cleavage.

Gasdermin-C is a human protein that functions as a precursor to the pore-forming protein Gasdermin-C, N-terminal (GSDMC-NT). Upon cleavage by caspase-8 in response to death signals, the N-terminal fragment binds to the inner leaflet of the plasma membrane, homooligomerizes, and forms large pores (10-15 nm in diameter), leading to pyroptosis. The full-length protein is primarily localized in the cytoplasm and cytosol, while the active N-terminal fragment translocates to the cell membrane as a multi-pass membrane protein. This recombinant fragment (residues 315-508) was selected computationally to provide a stable and soluble unit for investigating the protein's structural and functional properties, supporting research in cell death pathways and inflammatory responses.