Anti-Human ATG3 Antibody Pair

Product Description: Autophagy related 3 (ATG3) is a ubiquitin-like-conjugating enzyme essential for autophagy, a cellular degradation process. ATG3 catalyzes the conjugation of Atg8/LC3 to phosphatidylethanolamine, crucial for autophagosome formation. It contains an N-terminal domain, a catalytic domain with an active-site cysteine, and a C-terminal domain with a conserved FLKF motif. ATG3 interacts with ATG7 and ATG12-ATG5 complexes to facilitate LC3 lipidation. It also functions as a membrane curvature sensor, promoting LC3/GABARAP lipidation in areas of membrane stress. In disease contexts, ATG3 has been implicated in cancer progression, with its overexpression observed in human osteosarcoma cells enhancing autophagy. Additionally, ATG3 plays a role in neurodegenerative diseases, where its regulation of autophagy contributes to the degradation of accumulated proteins. Protein Function: E2 conjugating enzyme that catalyzes the covalent conjugation of the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to the amino group of phosphatidylethanolamine (PE)-containing lipids in the membrane resulting in membrane-bound ATG8-like proteins which is one of the key steps in the development of autophagic isolation membranes during autophagosome formation (PubMed:24191030, PubMed:33446636, PubMed:37252361). Cycles back and forth between binding to ATG7 for loading with the ATG8-like proteins and binding to E3 enzyme, composed of ATG12, ATG5 and ATG16L1 to promote ATG8-like proteins lipidation (PubMed:11825910, PubMed:12207896, PubMed:12890687, PubMed:16704426, PubMed:24186333). Also plays a role as a membrane curvature sensor that facilitates LC3/GABARAP lipidation by sensing local membrane stress associated with lipid-packing defects as occurs with high molar proportions of conical lipids or strident membrane curvature (By similarity). Interacts with negatively-charged membranes promoting membrane tethering and enhancing LC3/GABARAP lipidation (PubMed:29142222). Also acts as an autocatalytic E2-like enzyme by catalyzing the conjugation of ATG12 to itself in an ATG7-dependent manner, this complex thus formed, plays a role in mitochondrial homeostasis but not in autophagy (By similarity). ATG12-ATG3 conjugation promotes late endosome to lysosome trafficking and basal autophagosome maturation via its interaction with PDCD6IP (By similarity). ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation (By similarity). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (By similarity) [The Uniprot Consortium]