Recombinant ATG4C protein (His tag)

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This recombinant protein product features a 241-amino acid fragment (residues 187-427) of human Cysteine protease ATG4C, a key enzyme involved in autophagy regulation. The fragment is designed for structural and biochemical studies, offering a stable and soluble unit ideal for investigating protease mechanisms and protein interactions in autophagy pathways.

Cysteine protease ATG4C (AUT-like 3 cysteine endopeptidase) is an essential enzyme in autophagy, mediating both proteolytic activation and delipidation of ATG8 family proteins such as MAP1LC3 and GABARAPL2. Its protease activity cleaves the C-terminal amino acid of ATG8 proteins to expose a glycine residue, which is critical for conjugation to phosphatidylethanolamine (PE) and membrane insertion during autophagosome formation. ATG4C also catalyzes delipidation of PE-conjugated ATG8 proteins, with studies indicating it has stronger delipidation activity compared to other family members like ATG4B, though it plays a lesser role in phagophore growth during mitophagy. The protein is localized in the cytoplasm, where it contributes to the dynamic regulation of autophagy processes, making it a valuable target for research into cellular degradation mechanisms and related diseases.