Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins . The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine . Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine and insertion to membranes, which is necessary for autophagy . Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP . Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins : acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 . In addition to the protease activity, also mediates delipidation of ATG8 family proteins . Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy . 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 . Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy .

Cysteine protease ATG4A (EC 3.4.22.-) (AUT-like 2 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 2) (Autophagin-2) (Autophagy-related protein 4 homolog A) (HsAPG4A) (hAPG4A)

q8wyn0

Human,Mouse,Rat

WB,IHC

WB 1:1000-1:5000
IHC 1:100-1:200

~46 kD

Rabbit

50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Store at -20°C. Stable for 12 months from date of receipt.