Background: ATG8 is a ubiquitin-like protein in yeast required for autophagy (intracellular bulk protein degradation). Starved yeast cells take up their own cytoplasm into vacuoles through autophagic bodies. ATG8 is requiered for autophagy: modified by the serial action of ATG4, ATG7, and ATG3, and conjugated at the C terminus with phosphatidylethanolamine, to become the form essential for generation of autophagosomes. ATG8 interacts also with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the vacuolar v-SNARE protein NYV1. ATG8 is highly conserved, with apparent homologues in the worm, mammals and plants. In higher eukaryotes, ATG8 consists of a multigene family.
Description: Rabbit polyclonal to GABARAPL2
Immunogen: KLH conjugated synthetic peptide derived from GABARAPL2
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 13 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/100-200;
·Immunocytochemistry: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.