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Human Polyclonal ATG3 Primary Antibody for WB - ABIN1882157
Baehrecke: Autophagy: dual roles in life and death? in Nature reviews. Molecular cell biology 2005
Show all 6 Pubmed References
Authors confirmed that the effect of PVT1 promoting autophagy was dependent on regulating ATG3 expression. Further investigations revealed that PVT1 could upregulate autophagy-related gene 3 (ATG3) expression by acting as an endogenous sponge of miR-365, which was an inhibitor gene on ATG3 protein by targeting 3'UTR of ATG3 mRNA.
this study identified an amino acid motif in ATG3 causing eIF5A dependency for its efficient translation
ATG3 was targeted by miR-23a, suggesting that ATG3 is an autophagy-related competing endogenous RNA.
Results revealed that miR-16 was significantly downregulated, and ATG3 was significantly upregulated in non-small cell lung carcinoma (NSCLC) patient tissue samples. ATG3 was found to be a direct target of miR-16.
miR-155 silencing rescued autophagosome number in Mycobacterium tuberculosis infected dendritic cells and enhanced autolysosome fusion, thereby supporting a previously unidentified role of the miR-155 as inhibitor of ATG3 expression.
PTK2 inhibition-induced sustained levels of ATG3 were able to sensitize cancer cells to DNA-damaging agents.
Our data demonstrate that HOTAIR promotes the activation of autophagy in HCC cells by upregulating the expression of the autophagy-related genes ATG3 and ATG7.
ATG3 upregulation contributes to autophagy induced by the detachment of intestinal epithelial cells from the extracellular matrix, but promotes autophagy-independent apoptosis of the attached cells
Hidden Markov models were used to detect protein homology among the flexible regions of Atg3 homologs and importance of conserved regions evaluated by performing affinity capture experiments with human Atg3 deletion constructs; binding studies and competition experiments demonstrate that overlapping sites in the Atg3FR are important for E3 binding and E1 binding.
The region of human ATG3 that interacts with ATG7 is precisely identified using nuclear magnetic resonance.
ATG3 gene and its gene family may play an important role in transformation of myelodysplastic syndrome.
Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3.
13 residues of the ATG3 fragment form a short beta-strand followed by an alpha-helix on a surface area that is an exclusive binding site for ATG12.
caspase-8 overexpression led to Atg3 degradation and this event depended on caspase-8 enzymatic activity
These results unveil a role for ATG12-ATG3 in mitochondrial homeostasis and implicate the ATG12 conjugation system in cellular functions distinct from the early steps of autophagosome formation.
Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p
Murine Atg8L/Apg8L modification is mediated by human Atg3.
A thiol-dependent process is being reported that may account for impaired autophagy during aging. This is through direct oxidation of key autophagy-related (Atg) proteins Atg3 and Atg7.
These findings highlight a critical role of ATG3-dependent autophagy for mitochondrial homeostasis regulation in both pluripotency acquirement and maintenance.
miR-495 targets ATG3 and regulates its protein levels under starvation conditions. miR-495 also inhibits starvation-induced autophagy by decreasing the number of autophagosomes.
ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function.
Atg3 expression, similar to Atg5 expression, is required for Immunity Related GTPases and Guanylate binding proteins to dock to pathogen-containing vacuoles.
Vaccinia virus actively disrupts the cellular autophagy through a novel molecular mechanism that is associated with aberrant LC3 lipidation and a direct conjugation between ATG12 and ATG3.
The model and biochemical data provide a rationale for Atg7 dimerization: Atg8 is transferred in trans from the catalytic cysteine of one Atg7 protomer to Atg3 bound to the N-terminal domain of the opposite Atg7 protomer within the homodimer.
Autophagy is a process of bulk degradation of cytoplasmic components by the lysosome or vacuole. Human ATG3 displays the same enzymatic characteristics in vitro as yeast Apg3, a protein-conjugating enzyme essential for autophagy (Tanida et al., 2002
, autophagy-related protein 3
, ubiquitin-like-conjugating enzyme ATG3
, ATG3 autophagy related 3 homolog
, autophagy-related 3
, preconditioning-inducible gene 1 protein
, potential E2-like lipid conjugating enzyme Atg3