Anti-ATG13, Polyclonal [ATG13]
Invented by Dr Sharon Tooze from The Francis Crick Institute
Invented at Cancer Research UK London Research Institute: Lincoln's Inn Fields
- Datasheet
- References (2)
- Inventor Info
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![Image for Anti-ATG13, Polyclonal [ATG13]](https://res.cloudinary.com/ximbio/image/upload/c_limit,fl_lossy,h_282,q_auto,w_368/a32257c8-5a76-4fdf-9e25-1cb441f69c18.jpg)
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![Image thumbnail for Anti-ATG13, Polyclonal [ATG13]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/e3051f1a-ee09-4897-8bef-eccb056a0f7a.jpg)
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![Image thumbnail for Anti-ATG13, Polyclonal [ATG13]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/9badf0da-4aad-4f47-be38-19739837ab50.jpg)
| Catalogue Number | 151612 |
| Applications | WB |
| Antigen/Gene or Protein Targets | ATG13 |
| Reactivity | Human |
| Relevance | 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. Atg13 only binds in the unphosphorylated state, and its dephosphorylation has been shown to be TOR dependent. |
| Host | Rabbit |
| Immunogen | C-terminal synthetic peptide |
| Notes | This antibody is not available for licence, please refer to supplier information to find a source of the antibody. |
| Research Area | Apoptosis and Programmed Cell Death, Cancer, Cell Signaling & Signal Transduction, Metabolism |
References: 2 entries
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.
Europe PMC ID: 18936157
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References: 2 entries
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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