Phospho-Optineurin (Ser177) Antibody #57548
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 75 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Phospho-Optineurin (Ser177) Antibody recognizes endogenous levels of optineurin protein only when phosphorylated at Ser177.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Ser177 of human optineurin protein.
Background
Optineurin is a signaling protein involved in maintenance of the Golgi complex, membrane trafficking, NF-κB, and interferon signaling. Mutations in the gene encoding optineurin have been associated with human diseases including glaucoma, Paget disease of bone, and amyotrophic lateral sclerosis (ALS) (1-2). Optineurin is thought to contribute to these pathologies through regulation of inflammatory signaling, autophagy, and mitophagy (1, 3). The NF-κB-activating kinase/TANK-binding kinase 1 (NAK/TBK1) phosphorylates optineurin at serine 177, regulating optineurin’s role in autophagy and mitophagy (4-6). The tumor suppressor HACE1 ubiquitylates optineurin, promoting the interaction of optineurin with the autophagy receptor p62/SQSTM1 (7).
Phosphorylation of optineurin at serine 177 by TBK1 enhances binding to LC3 and promotes autophagic clearance (8). Additional studies also suggest that serine 177 is phosphorylated during mitosis by PLK1 (9). In addition to serine 177, TBK1 also phosphorylates optineurin at serine 473 and 513, which can enhance its binding to ubiquitin chains and promote mitophagy (5, 6).
Phosphorylation of optineurin at serine 177 by TBK1 enhances binding to LC3 and promotes autophagic clearance (8). Additional studies also suggest that serine 177 is phosphorylated during mitosis by PLK1 (9). In addition to serine 177, TBK1 also phosphorylates optineurin at serine 473 and 513, which can enhance its binding to ubiquitin chains and promote mitophagy (5, 6).
- Ying, H. and Yue, B.Y. (2016) Exp Eye Res 144, 73-80.
- Slowicka, K. et al. (2016) Trends Immunol 37, 621-33.
- Markovinovic, A. et al. (2017) Prog Neurobiol 154, 1-20.
- Moore, A.S. and Holzbaur, E.L. (2016) Proc Natl Acad Sci U S A 113, E3349-58.
- Richter, B. et al. (2016) Proc Natl Acad Sci U S A 113, 4039-44.
- Heo, J.M. et al. (2015) Mol Cell 60, 7-20.
- Liu, Z. et al. (2014) Cancer Cell 26, 106-20.
- Wild, P. et al. (2011) Science 333, 228-33.
- Kachaner, D. et al. (2012) Mol Cell 45, 553-66.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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