ATG4D Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, IF, E |
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Primary Accession | Q86TL0 |
Other Accession | NP_116274, 27903825 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | Predicted: 52 kDa Observed: 49 kDa |
Application Notes | ATG4D antibody can be used for detection of ATG4D by Western blot at 1 - 2 µg/ml. Antibody can also be used for immunohistochemistry starting at 5 µg/mL. For immunofluorescence start at 20 µg/mL. |
Gene ID | 84971 |
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Target/Specificity | ATG4D; ATG4D antibody is human, mouse and rat reactive. At least two isoforms of ATG4D are known to exist; this antibody will detect only the larger isoform. ATG4D is predicted to not cross-react with other ATG4 proteins. |
Reconstitution & Storage | ATG4D antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
Precautions | ATG4D Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ATG4D {ECO:0000303|PubMed:19549685, ECO:0000312|HGNC:HGNC:20789} |
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Function | [Cysteine protease ATG4D]: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:21177865, PubMed:29458288, PubMed:30661429). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (PubMed:21177865). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:29458288, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:29458288, PubMed:33909989). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). ATG4D plays a role in the autophagy-mediated neuronal homeostasis in the central nervous system (By similarity). Compared to other members of the family (ATG4A, ATG4B or ATG4C), constitutes the major protein for the delipidation activity, while it promotes weak proteolytic activation of ATG8 proteins (By similarity). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore- endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106). |
Cellular Location | [Cysteine protease ATG4D]: Cytoplasm |
Tissue Location | Widely expressed in testis. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components (1,2). ATG4D, also known as AUTL4, is one of four mammalian orthologs of the yeast ATG4 protein; all four are cysteine proteases (3). ATG4 is required for ATG8 conjugation to phosphatidylethanolamine on autophagosomal membranes. In mammals, each ATG4 homolog shows a selective preference for the ATG8 homologs (4).
References
Gozuacik D and Kimchi A. Autophagy as a cell death and tumor suppressor mechanism. Oncogene 2004; 23:2891-906.
Kisen GO, Tessitore L, Costelli P, et al. Reduced autophagic activity in primary rat hepatocellular carcinoma and ascites hepatoma cells. Carcinogenesis 1993; 14:2501-5.
Marino G, Uria JA, Puente XS, et al. Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy. J. Biol. Chem. 2003; 278:3671-8.
Li M, Hou Y, Wang J, et al. Kinetic comparisons of mammalian Atg4 homologues indicate selective preferences towards diverse Atg8 substrates. J. Biol. Chem. 2011; 286:7327-38.
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