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ATG3 Antibody Blocking peptide
Synthetic peptide
- SPECIFICATION
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- BACKGROUND
| Primary Accession | Q9NT62 |
|---|---|
| Clone Names | 70226124 |
| Gene ID | 64422 |
|---|---|
| Other Names | Ubiquitin-like-conjugating enzyme ATG3, 632-, Autophagy-related protein 3, APG3-like, hApg3, Protein PC3-96, ATG3, APG3, APG3L |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1807d was selected from the Y160 region of human APG3L. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ATG3 (HGNC:20962) |
|---|---|
| Synonyms | APG3, APG3L |
| 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:37252361, PubMed:33446636). 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:12207896, PubMed:24186333, PubMed:11825910, PubMed:12890687, PubMed:16704426). 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). |
| Cellular Location | Cytoplasm. |
| Tissue Location | Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta |
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Provided below are standard protocols that you may find useful for product applications.
Background
APG3L is an E2-like conjugating enzyme facilitating covalent binding of APG8(MAP1LC3) to phosphatidylethanolamine (PE). APG7 (an E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with APG3. Formation of the PE conjugate is essential for autophagy.Macroautophagy is the major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane bound autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane bound structure, which then fuse with the lysosome (or vacuole) releasing a single-membrane bound autophagic bodies which are then degraded within the lysosome (or vacuole).
References
Baehrecke EH. Nat Rev Mol Cell Biol. 6(6):505-10. (2005) Lum JJ, et al. Nat Rev Mol Cell Biol. 6(6):439-48. (2005) Greenberg JT. Dev Cell. 8(6):799-801. (2005) Levine B. Cell. 120(2):159-62. (2005) Shintani T and Klionsky DJ. Science. 306(5698):990-5. (2004)
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