Autophagy has been implicated in a number of medical contexts, such as cancer, neurodegeneration, and immunity.
| Inventor | Institute |
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| Sharon Tooze | Cancer Research UK, London Research Institute: Lincoln's Inn Fields |
| SKU: | 151612 |
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| Product description: | Atg13 only binds in the unphosphorylated state, and its dephosphorylation has been shown to be TOR dependent. |
| Conjugation: | Unconjugated |
| Immunogen: | C-terminal synthetic peptide |
| Cat. #: | 151612 |
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| Provenance and Ownership: | The Anti-ATG13 [ATG13] is owned by Cancer Research UK. CancerTools supplies the Anti-ATG13 [ATG13] under licence from Cancer Research UK and is the authorised source for its distribution. Sourcing Anti-ATG13 [ATG13] directly from the IP owner ensures authenticity, provenance and compliance with all applicable licensing and research use requirements. |
| Tool sub type: | Primary antibody |
| Unit size: | 100 ug |
| Research Fields: | Apoptosis and autophagy; Cancer; Cell signaling and signal transduction; Metabolism |
| Application: | WB |
| Target: | ATG13 |
| Reactivity: | Human |
| Clone: | ATG13 |
| Host: | Rabbit |
| Class: | Polyclonal |
| Target background: | Autophagy has been implicated in a number of medical contexts, such as cancer, neurodegeneration, and immunity. The serine-threonine protein kinase Atg1 was originally identified as a critical autophagy regulator in yeast. Full kinase activity of Atg1 in yeast requires its binding partners Atg13 and Atg17. |
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| Format: | Liquid |
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| Shipping conditions: | Dry ice |
| References: |
Chan et al. 2009. Mol Cell Biol. 29(1):157-71. PMID: 18936157. Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism. |
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