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ATG7 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 5
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | O95352 |
| Other Accession | Q641Y5, Q9D906 |
| Reactivity | Human, Mouse |
| Predicted | Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 77960 Da |
| Antigen Region | 22-51 aa |
| Gene ID | 10533 |
|---|---|
| Other Names | Ubiquitin-like modifier-activating enzyme ATG7, ATG12-activating enzyme E1 ATG7, Autophagy-related protein 7, APG7-like, hAGP7, Ubiquitin-activating enzyme E1-like protein, ATG7, APG7L |
| Target/Specificity | This ATG7 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 22-51 amino acids from the N-terminal region of human ATG7. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | ATG7 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATG7 (HGNC:16935) |
|---|---|
| Synonyms | APG7L |
| Function | E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Facilitates LC3-I lipidation with phosphatidylethanolamine to form LC3-II which is found on autophagosomal membranes (PubMed:34161705). Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Also plays a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (By similarity). |
| Cellular Location | Cytoplasm. Preautophagosomal structure. Note=Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme |
| Tissue Location | Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. |
Provided below are standard protocols that you may find useful for product applications.
Background
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). APG7 functions as an E1 enzyme essential for multisubstrates such as GABARAPL1 and ATG12. 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.
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) Tanida I., et al. Biochem. Biophys. Res. Commun. 292:256-262(2002) Tanida I., et al. J. Biol. Chem. 277:13739-13744(2002)
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