Anti-Cysteine protease ATG4A ATG4A Antibody

Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components (1,2) . ATG4A, also known as AUTL2, is one of four mammalian orthologs of the yeast ATG4 protein; all four are cysteine proteases (3) . ATG4 is required for ATG8 conjugation to phosphatidylethanolamine on autophagosomal membranes. In mammals, each ATG4 homolog shows a selective preference for the ATG8 homologs (4) .

ATG4A antibody is human, mouse and rat reactive. At least two isoforms of ATG4A are known to exist; this antibody will detect both isoforms. ATG4A is predicted to not cross-react with other ATG4 proteins.

ATG4A antibody was raised against an 18 amino acid peptide near the carboxy terminus of human ATG4A. The immunogen is located within the last 50 amino acids of ATG4A.

Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Has also an activity of delipidating enzyme for the PE-conjugated forms.