Anti-ULK1 Antibody

ULK1, also known as ATG1, is a key serine/threonine protein kinase probably acting at the most upstream step of autophagosome formation. Knockout of ULK1 results in a severe defect in the autophagy pathway. ULK1 is highly conserved among eukaryotes, and are the Unc-51-like kinases, ULK1 and ULK2 in mammals. ULK1 is ubiquitously expressed and involved in autophagy in response to starvation. It is the target of the TOR kinase signaling pathway that regulates autophagy through the control of phosphorylation status of ATG13. ULK1 also plays a role early in neuronal differentiation.

Two alternatively spliced transcript variants encoding different isoforms have been identified. ULK1 antibody is predicted to not cross-react with ULK2.

ULK1 antibody was raised against a 16 amino acid peptide near the center of human ULK1 . The immunogen is located within amino acids 350 - 400 of ULK1.

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 negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. May also phosphorylate SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165) .

Cytoplasm, cytosol . Preautophagosomal structure . Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. .