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ATG4C Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
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- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q96DT6 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 52497 Da |
| Antigen Region | 33-62 aa |
| Gene ID | 84938 |
|---|---|
| Other Names | Cysteine protease ATG4C, 3422-, AUT-like 3 cysteine endopeptidase, Autophagin-3, Autophagy-related cysteine endopeptidase 3, Autophagy-related protein 4 homolog C, ATG4C, APG4C, AUTL1, AUTL3 |
| Target/Specificity | This ATG4C antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 33-62 amino acids from the N-terminal region of human ATG4C. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 |
| 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 | ATG4C Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATG4C {ECO:0000303|PubMed:21177865, ECO:0000312|HGNC:HGNC:16040} |
|---|---|
| Function | 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). 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). In contrast to other members of the family, weakly or not involved in phagophore growth during mitophagy (PubMed:33773106). |
| Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Macroautophagy is the major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane bound autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane bound structure, which then fuse with the lysosome (or vacuole) releasing a single-membrane bound autophagic bodies which are then degraded within the lysosome (or vacuole). APG4 is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.
References
Baehrecke EH. Nat Rev Mol Cell Biol. 6(6):505-10. (2005)
Lum JJ, et al. Nat Rev Mol Cell Biol. 6(6):439-48. (2005)
Greenberg JT. Dev Cell. 8(6):799-801. (2005)
Levine B. Cell. 120(2):159-62. (2005)
Shintani T and Klionsky DJ. Science. 306(5698):990-5. (2004)
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