GABARAPL1 (D5R9Y) XP^® Rabbit mAb recognizes endogenous levels of total GABARAPL1 protein. This antibody does not cross react with other GABARAP family members.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human GABARAPL1 protein.

GABA_A receptor associated protein (GABARAP) is an Atg8 family protein with a key role in autophagy, which was originally discovered as a protein associated with the GABA_A receptor regulating receptor trafficking to the plasma membrane (1). Proteins in this family, including microtubule-associated protein light chain 3 (LC3) and GATE-16 (GABARAPL2), become incorporated into the autophagosomal membranes following autophagic stimuli such as starvation (2). Like the other family members, GABARAP is cleaved at its carboxyl terminus, which leads to conjugation by either of the phospholipids phosphatidylethanolamine or phosphatidylserine (3,4). This processing converts GABARAP from a type I to a type II membrane bound form involved in autophagosome biogenesis. Processing of GABARAP involves cleavage by Atg4 family members (5,6) followed by conjugation by the E1 and E2 like enzymes Atg7 and Atg3 (7,8). GABARAPL1/GEC1, a protein that is highly related to GABARAP, was identified as an estrogen inducible gene, and is also associated with autophagosomes (9-11).
Gamma-aminobutyric acid receptor-associated protein-like 1 (GABARAPL1) appears to be more highly expressed in the CNS as compared to other family members (12-14). Expression of GABARAPL1 is associated with prognosis of some cancers, including hepatocellular and breast cancer (15,16). Inhibition of GABARAPL1 expression in breast cancer cells attenuates autophagic flux, results in metabolic changes, and leads to cancer promoting activities (17).