Recombinant ATG4B protein (His tag)

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Recombinant Human ATG4B (Amino acids 1-357) is a high-purity, biologically active fragment of the cysteine protease ATG4B, a key regulator of autophagy. This fragment represents a stable and soluble unit ideal for structural studies, biochemical assays, and autophagy research applications.

ATG4B is a crucial cysteine protease that plays a central role in multiple forms of autophagy, including canonical autophagy (macroautophagy), non-canonical autophagy, and mitophagy. Its primary function involves the proteolytic activation of ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2, and GABARAP) by cleaving their C-terminal amino acid to expose a glycine residue, which is essential for conjugation to phosphatidylethanolamine and membrane insertion during autophagosome formation. Additionally, ATG4B mediates delipidation of PE-conjugated ATG8 proteins and acts as a deubiquitinating-like enzyme to remove ATG8 conjugated to other proteins. The protein localizes primarily to the cytoplasm and cytosol, with smaller portions found in autophagosomes, endoplasmic reticulum, and mitochondria, where it regulates ATG9A trafficking and promotes phagophore-endoplasmic reticulum contacts during mitophagy.