Product Details
| Alternative Name: | Gamma-aminobutyric acid receptor-associated protein |
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| MW: | ~42.1kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | O95166 |
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| Formulation: | Liquid. In PBS. |
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| Purity: | ≥90% (SDS-PAGE) |
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| Application Notes: | For use in general and selective autophagy studies. |
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| Shipping: | Dry Ice |
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| Short Term Storage: | -80°C |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Stable for at least 12 months after receipt when stored at -80°C.  |
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| Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | Autophagy is a highly conserved bulk protein degradation pathway responsible for the turnover of long-lived proteins, disposal of damaged organelles, and clearance of aggregate-prone proteins. Autophagy is involved in various physiological or pathological processes, such as development, host defense response, cancer and neuronal degenerative diseases. It involves concerted action of more than 20 specific autophagy (ATG) proteins that mediate the formation of a double-membrane vesicle, the autophagosome, which engulfs the substrate and delivers it to the lysosome for degradation.
Formation and expansion of the pre-autophagosomal structure in yeast requires the attachment of the ubiquitin-like protein ATG8 via its C-terminal glycine to the amino group of phosphatidylethanolamine (PE), enabling its anchoring to the isolation membrane of the autophagosome. In mammals, ATG8 is represented by at least seven related proteins that fall into two subgroups, LC3- and GABARAP-like proteins. The free and PE linked versions of these proteins are often referred to as LC3-I and LC3-II respectively. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE image (coomassie stained) of GST-GABARAP (2.5µg, BML-UW1175).
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General Literature References
Fighting disease by selective autophagy of aggregate-prone proteins: H. Knaevelsrud & A. Simonsen; FEBS Lett.
584, 2635 (2010),
Abstract;
Role of autophagy in suppression of inflammation and cancer: E. White, et al. ; Curr. Opin. Cell. Biol.
22, 212 (2010),
Abstract;
A role for ubiquitin in selective autophagy: V. Kirkin, et al.; Mol.Cell.
34, 259 (2009),
Abstract;
Autophagy as an emerging dimension to adaptive and innate immunity: S. Hussey, et al.; Semin. Immunol.
21, 233 (2009),
Abstract;
The emerging role of autophagy in Parkinson's disease: Z.H. Cheung, et al.; Mol. Brain Res.
2, 29 (2009),
Abstract;
Autophagy fights disease through cellular self-digestion: M. Mizushima, et al.; Nature
451, 1069 (2008),
Abstract;
Autophagosome formation: core machinery and adaptations: Z. Xie, et al.; Nat. Cell. Biol.
9, 1102 (2007),
Abstract;
Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B: H. He, et al.; J. Biol. Chem
278, 29278 (2003),
Abstract;
Autophagy in the eukaryotic cell: F. Reggiori, et al.; Eukaryot. Cell.
1, 11 (2002),
Abstract;
Cloning, expression patterns, and chromosome localization of three human and two mouse homologues of GABA(A) receptor-associated protein: Y. Xin, et al.; Genomics
744, 408 (2001),
Abstract;
