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.