GABARAPL2 (also known as Golgi-associated ATPase enhancer of 16 kDa; GATE-16) was originally characterized as a factor essential for intra-Golgi protein transport. Later GABARAPL2 along with LC3 and GABARAP, were identified as the homologs of yeast ATG8 which is a unique ubiquitin-like protein essential for autophagy. When induced GABARAPL2 is first digested by ATG4 family enzymes to become its mature form: GABARAPL2-I, later conjugated to PE lipid as lipidated form: GABARAPL2-II. The lipidated form migrates faster than its mature form on SDS-PAGE gel. GABARAPL2 is strongly expressed in the brain. This antibody, generated against the full-length of GABARAPL2, is specific to GABARAPL2. It does not recognize recombinant GABARAP as well as GABARAPL1.