Anti-Cysteine protease ATG4C ATG4C 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) . ATG4C, also known as autophagin-3, is one of four mammalian orthologs of the yeast ATG4 protein; all four are cysteine proteases (3) . Recent studies have shown that ATG4C and Beclin-1 are regulated by the microRNA miR-376b; overexpression of miR-376b led to decreased mRNA and protein levels, thereby blocking starvation and TOR inhibition-related autophagy (4) .

ATG4C antibody was raised against an 18 amino acid peptide near the carboxy terminus of human ATG4C. The immunogen is located within the last 50 amino acids of ATG4C.

Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Is not essential for autophagy development under normal conditions but is required for a proper autophagic response under stressful conditions such as prolonged starvation (By similarity) . Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, 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.