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APG4D Antibody (Center S341)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q86TL0 |
| Other Accession | Q684M2, Q8BGV9, NP_116274.3 |
| Reactivity | Human |
| Predicted | Mouse, Pig |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 52922 Da |
| Antigen Region | 321-346 aa |
| Gene ID | 84971 |
|---|---|
| Other Names | Cysteine protease ATG4D, 3422-, AUT-like 4 cysteine endopeptidase, Autophagin-4, Autophagy-related cysteine endopeptidase 4, Autophagy-related protein 4 homolog D, Cysteine protease ATG4D, mitochondrial, ATG4D, APG4D, AUTL4 |
| Target/Specificity | This APG4D antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 321-346 amino acids from the Central region of human APG4D. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | APG4D Antibody (Center S341) 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} |
|---|---|
| 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 is the process by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is postulated to be essential for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. Reduced levels of autophagy have been described in some malignant tumors, and a role for autophagy in controlling the unregulated cell growth linked to cancer has been proposed. This gene encodes a member of the autophagin protein family. The encoded protein is also designated as a member of the C-54 family of cysteine proteases.
References
Betin, V.M., et al. J. Cell. Sci. 122 (PT 14), 2554-2566 (2009) :
Lamesch, P., et al. Genomics 89(3):307-315(2007)
Marino, G., et al. J. Biol. Chem. 278(6):3671-3678(2003)
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