Anti-Cysteine protease ATG4B ATG4B 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) . ATG4B, also known as AUTL1, 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) . ATG4B has been found to be a novel protective protein in inflammatory colitis (5) .

ATG4B antibody is human, mouse and rat reactive. At least two isoforms of ATG4B are known to exist; this antibody will detect only the larger isoform. ATG4B is predicted to not cross-react with other ATG4 proteins.

ATG4B antibody was raised against a 17 amino acid peptide near the carboxy terminus of human ATG4B. The immunogen is located within the last 50 amino acids of ATG4B.

Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, 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. Has also an activity of delipidating enzyme for the PE-conjugated forms.