Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Atg101 Antibody recognizes endogenous levels of total Atg101 protein. This antibody also detects a 55 kDa protein of unknown origin in some cell lines.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val177 of human Atg101 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Atg101 was discovered as a binding protein for Atg13, a component of the ULK1 serine-threonine kinase complex required for autophagy (1-3). Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (4,5). It is generally activated by conditions of nutrient deprivation, but is also associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (6). The molecular machinery of autophagy was largely discovered in yeast and is directed by a number of autophagy-related (Atg) genes. The ULK1 complex includes both Atg13 and FIP200 and is required for starvation-induced autophagy (7-9). Interaction between Atg101 and Atg13 can be important for the stability and basal phosphorylation of Atg13 and ULK1 (1,2).
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