Rabbit Polyclonal Phospho-ULK2(S323) Antibody

The Phospho-ULK2 (S323) antibody detects ULK2 (Unc-51-like kinase 2) when phosphorylated at serine 323. a post-translational modification critical for regulating its role in autophagy. ULK2. a serine/threonine kinase homologous to ULK1. is a key initiator of autophagy, coordinating cellular responses to nutrient deprivation, energy stress, or other autophagy-inducing signals. Phosphorylation at specific residues, including S323. modulates ULK2 activity through interactions with upstream regulators like mTOR (mechanistic target of rapamycin) and AMP-activated protein kinase (AMPK). Under nutrient-rich conditions, active mTOR phosphorylates ULK2. suppressing its kinase activity and inhibiting autophagy. During stress, mTOR inhibition or AMPK activation promotes ULK2 dephosphorylation/phosphorylation at distinct sites, triggering autophagosome formation. The S323 phosphorylation site is implicated in ULK2’s subcellular localization, interaction partners, or enzymatic activation, though its precise mechanistic role remains under investigation. The Phospho-ULK2 (S323) antibody is widely used in autophagy research to study ULK2 activation dynamics, particularly in models of metabolic stress, neurodegenerative diseases, or cancer. Specific validation (e.g., knockout/knockdown controls, phospho-mutants) is essential to confirm antibody specificity, as cross-reactivity with ULK1 or other phospho-proteins may occur. This tool helps elucidate ULK2’s regulatory networks and its therapeutic relevance in autophagy-related disorders.