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ATG4A Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q8WYN0 |
| Other Accession | NP_443168, 30795252 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | Predicted: 48 kDa Observed: 44 kDa |
| Application Notes | ATG4A antibody can be used for detection of ATG4A by Western blot at 1 - 2 µg/ml. Antibody can also be used for immunohistochemistry starting at 5 µg/mL. |
| Gene ID | 115201 |
|---|---|
| Target/Specificity | ATG4A; ATG4A antibody is human, mouse and rat reactive. At least two isoforms of ATG4A are known to exist; this antibody will detect both isoforms. ATG4A is predicted to not cross-react with other ATG4 proteins. |
| Reconstitution & Storage | ATG4A antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
| Precautions | ATG4A Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATG4A {ECO:0000303|Ref.20, ECO:0000312|HGNC:HGNC:16489} |
|---|---|
| Function | Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15169837, PubMed:12473658, PubMed:17347651, PubMed:21177865, PubMed:21245471, PubMed:22302004, PubMed:32732290). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (PubMed:15169837, PubMed:12473658, PubMed:17347651, PubMed:21177865, PubMed:21245471, PubMed:22302004). 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 (PubMed:15169837, PubMed:12473658, PubMed:17347651, PubMed:21177865, PubMed:21245471, PubMed:22302004). Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP (PubMed:15169837, PubMed:12473658, PubMed:17347651, PubMed:21177865, PubMed:21245471, PubMed:22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating- like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106). 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). Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity (PubMed:29458288). 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 | Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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). ATG4A, also known as AUTL2, 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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