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Western blot(SDS PAGE) analysis of extracts from K562 cells.Using ATG3Rabbit mAb [4LE6] at dilution of 1:1000 incubated at 4℃ over night.
Protein names :ATG3,APG3,APG3L,ATG3_HUMAN,Ubiquitin-like-conjugating enzyme ATG3
UniProtID :Q9NT62
MASS(da) :35,864
MW(kDa) :40 kDa
Form :Liquid
Purification :Protein A purification
Host :Rabbit
Isotype :IgG
sensitivity :Endogenous
Reactivity :Human
Specificity :Antibody is produced by immunizing animals with a synthetic peptide at the sequence of human ATG3
Storage :Antibody store in 10 mM PBS, 0.5mg/ml BSA, 50% glycerol. Shipped at 4°C. Store at-20°C or -80°C. Products are valid for one natural year of receipt.Avoid repeated freeze / thaw cycles.
WB Positive detected :K562 cells
Function : 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 membrane 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 removing OFD1 from centriolar satellites via the autophagic pathway..
Tissue specificity :Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta..
Subcellular locationi :Cytoplasm.
IMPORTANT: For western blots, incubate membrane with diluted primary antibody in 1% w/v BSA, 1X TBST at 4°C overnight.