Anti-ULK2 Antibody

ULK2, also known as ATG1B, is a key serine/threonine protein kinase probably acting at the most upstream step of autophagosome formation. Knockout of ULK2 results in a severe defect in the autophagy pathway. ULK2 is highly conserved among eukaryotes and shows high homology with its related protein ULK1. Both ULK1 and ULK2 form a complex with ATG13 and FIP200 that mediates TOR signaling and is essential for autophagy. Like ULK1, ULK2 is also thought to be involved in early neuronal growth and differentiation.

ULK2 antibody was raised against a 17 amino acid peptide near the center of human ULK2 . The immunogen is located within amino acids 480 - 530 of ULK2.

Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3- kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons.