Anti-Atg4C Antibody

EC 3.4.22.-, AUT-like 3 cysteine endopeptidase, Autophagy-related cysteine endopeptidase 3, Autophagin-3, Autophagy-related protein 4 homolog C, HsAPG4C

Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:21177865, PubMed:29458288, PubMed:30661429). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (PubMed:21177865). 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 (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:29458288, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:29458288, PubMed:33909989). Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity (PubMed:29458288). In contrast to other members of the family, weakly or not involved in phagophore growth during mitophagy (PubMed:33773106). {UniProtKB:Q9Y4P1, PubMed:21177865, PubMed:29458288, PubMed:30661429, PubMed:33773106, PubMed:33909989}.

Immunoblotting: use at 1-2ug/mL. A band of ~52kDa is detected. <br><br>These are recommended concentrations. <br><br>Endusers should determine optimal concentrations for their applications.

Autophagy is a catabolic process that results in the degradation of bulk cytoplasmic contents within autophagosomes and lysosomes. Atg4C is a homolog of yeast Apg4, a cysteine protease involved in autophagy. The deduced 458-amino acid protein contains a putative active-site cysteine at position 110. Atg4C shares significant similarity with yeast Apg4, except for divergence at its N- and C-terminal ends. The absence of an N-terminal signal sequence suggests that Atg4C is a cytoplasmic enzyme. Northern blot analysis detected a 3.5-kb transcript in many tissues, with highest expression in skeletal muscle, heart, liver, and testis. It was also detected in some tumor cell lines, but not in fetal tissues.