APG8 / ATG8 antibody

Principal name

APG8 / ATG8 antibody

Alternative names for APG8 / ATG8 antibody

AUT7, CVT5, Autophagy-related protein 8, Autophagy-related ubiquitin-like modifier ATG8, Cytoplasm to vacuole targeting protein 5

SwissProt ID

P38182 (Yeast)

Gene ID

852200 (ATG8)

Available reactivities

Ye (Yeast), S. cerevisiae (Saccharomyces cerevisiae)

Available hosts


Available applications

Enzyme Immunoassay (E), Western blot / Immunoblot (WB)

Background of APG8 / ATG8 antibody

Ubiquitin-like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin. Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg8 and Apg12. Proteins of the second class include parkin, RAD23 and DSK2, are designated ubiquitin-domain proteins (UDPs). These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other. In contrast to UBLs, UDPs are not conjugated to other proteins. Apg8 is required for autophagy (intracellular bulk protein degradation) in yeast. Starved yeast cells take up their own cytoplasm into vacuoles through autophagic bodies. Autophagic bodies form a double-membraned structure called the autophagosome, which subsequently fuses with the vacuole/lysosome. This process similar in mammals. Two sets of genes, APG and AUT, have been identified with this process, and are responsible for two ubiquitin-like systems Apg12 and Apg8, respectively. Apg12 is synthesized in its mature form and seems to have one target, Apg5. Almost all Apg12 molecules are conjugated with Apg5. Aut2/Apg4 processes the Apg8/Aut7 system at its carboxy-terminal region. Apg8 exists in two forms, one is membrane bound through a phospholipid. Lipidation/ activation of Apg8 is mediated by Apg7 and transferred to Apg3 and finally forms a conjugate with phosphatidyl-ethanolamine (PE). Apg4 cleaves Apg8-PE, releasing Apg8 from membrane. Morphological studies show that Apg8 localizes on the membrane of intermediate structures of the autophagosome; this transient association seems to be essential for formation of the autophagosome. Both Apg12 and Apg8 are highly conserved, with apparent homologues in the worm, mammals and plants. In higher eukaryotes, Apg8 consists of a multigene family.

General readings

1. Kirisako T, Baba M, Ishihara N, Miyazawa K, Ohsumi M, Yoshimori T, Noda T, Ohsumi Y. (1999) Formation process of autophagosome is traced with Apg8/Aut7p in yeast.
J Cell Biol.;147(2):435-46.
2. Ohsumi, Y. (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nature Reviews Molecular Cell Biology 2, 211 -216.
3. Liakopoulos D et al. (1998). A novel protein modification pathway related to the ubiquitin system.
EMBO J. 15;17(8):2208-14.
4. Jentsch S, Pyrowolakis G. (2000) Ubiquitin and its kin: how close are the family ties.
Trends Cell Biol. 10(8):335-42.
5. Marino, G. et al., (2003) , Human Autophagins, a Family of Cysteine Proteinases Potentially Implicated in Cell Degradation by Autophagy.
J. Biol. Chem.,278: 6, 3671-3678.

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Primary Antibodies

Catalog No. Host Iso. Clone Pres. React. Applications  

APG8 / ATG8 antibody

Figure 1. Immunoblot of APG8 fusion protein. Anti-APG8 antibody generated by immunization with recombinant yeast APG8 was tested by immunoblot with other anti-UBL antibodies against E.coli lysates expressing the APG8-GFP fusion protein. All UBLs possess limited homology to Ubiquitin and to each other, therefore it is important to know the degree of reactivity of each antibody against each UBL. Panel A shows total protein staining using ponceau. Panel B shows specific reaction with APG8 using a 1:4,000 and 1:8,000 dilution of IgG fraction of Rabbit-anti-APG8 (Yeast) followed by reaction with a 1:15,000 dilution of HRP Goat-a-Rabbit IgG MX. All primary antibodies were diluted in TTBS buffer supplemented with 5% non-fat milk and incubated with the membranes overnight at 4° C. E.coli lysate proteins were separated by SDS-PAGE using a 15% gel. Similar experiments (data not shown), where other UBL fusion proteins were separated and probed with this antibody showed no reactivity of anti-APG8 with other UBLs. This data indicates that anti-APG8 is highly specific and does not cross react with other UBLs. A chemiluminescence system was used for signal detection (Roche). Other detection systems will yield similar results. Data contributed by M. Malakhov, www.lifesensors.com, personal communication. Rabbit Purified Ye E, WB
0.5 mg / €510.00
  Acris Antibodies GmbH

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