ATG3
宿主: 人
宿主: 大肠杆菌(E. Coli)
Recombinant
Greater than 95 % as determined by reducing SDS-PAGE.
ELISA, WB, SDS, MS
应用备注
Optimal working dilution should be determined by the investigator.
限制
仅限研究用
状态
Liquid
浓度
0.1-2 mg/mL
缓冲液
20 mM Tris-HCl based buffer, pH 8.0
储存条件
-80 °C,4 °C,-20 °C
储存方法
Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
atg3 Protein, im:6910145 Protein, wu:fb15g12 Protein, zgc:64156 Protein, APG3 Protein, APG3-LIKE Protein, APG3L Protein, PC3-96 Protein, 2610016C12Rik Protein, Apg3l Protein, Atg3l Protein, PIG-1 Protein, Pig1 Protein, ATATG3 Protein, K11J9.1 Protein, K11J9_1 Protein, autophagy related 3 Protein, autophagy 3 (APG3) Protein, similar to S. cerevisiae ATG3 (YNR007C) part of ubiquitin-like system that mediates Atg8-phosphatidylethanolamine conjugation required for protein-vacuolar targeting and autophagy Protein, atg3 Protein, ATG3 Protein, Atg3 Protein
背景
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the mbrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by roving OFD1 from centriolar satellites via the autophagic pathway.