ATG4A Research Reagents

Cysteine protease ATG4A is a protein in humans that is encoded by ATG4A gene. 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.

The following ATG4A reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

ATG4A Antibodies

ATG4A Antibodies for Homo sapiens (Human)

ATG4A Antibodies for Arabidopsis thaliana (Mouse-ear cress)

ATG4A Antibodies for Oryza sativa subsp. japonica (Rice)

ATG4A Antibodies for Oryza sativa subsp. indica (Rice)

ATG4A Proteins

ATG4A Proteins for Oryza sativa subsp. indica (Rice)

ATG4A Proteins for Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)

ATG4A Proteins for Gallus gallus (Chicken)

ATG4A Proteins for Bos taurus (Bovine)

ATG4A Proteins for Xenopus laevis (African clawed frog)

ATG4A Proteins for Oryza sativa subsp. japonica (Rice)

ATG4A Proteins for Mus musculus (Mouse)

ATG4A Proteins for Arabidopsis thaliana (Mouse-ear cress)

ATG4A Proteins for Homo sapiens (Human)

ATG4A Background

Cysteine protease ATG4A is a protein in humans that is encoded by the ATG4A gene. 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. Its preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. It has also activity of the delipidating enzyme for the PE-conjugated forms.

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