The Phospho-AMPK alpha 1 (Ser496) antibody is a specialized tool used to detect the activated form of AMP-activated protein kinase (AMPK) alpha 1 subunit phosphorylated at serine residue 496. AMPK is a critical energy-sensing kinase that regulates cellular metabolism by responding to fluctuations in ATP levels. It consists of three subunits: alpha (catalytic), beta, and gamma (regulatory). The alpha subunit exists in two isoforms (alpha 1 and alpha 2), with alpha 1 being ubiquitously expressed. Phosphorylation at specific sites, such as Thr172 in the activation loop, is essential for AMPK activation. However, phosphorylation at Ser496 (human isoform numbering) has been identified as a regulatory modification, potentially influencing AMPK activity, localization, or interactions with other proteins. Studies suggest this site may be targeted by kinases such as AKT or PKA under certain metabolic or stress conditions, linking AMPK signaling to broader pathways like insulin signaling or cellular survival. Researchers employ this antibody to investigate AMPK alpha 1 activation dynamics in contexts like metabolic disorders (e.g., diabetes, obesity), cancer (where AMPK modulates cell proliferation), or autophagy regulation. Its applications span Western blotting, immunofluorescence, and immunohistochemistry, aiding in the characterization of AMPK-related signaling in tissues or cultured cells under energy-stress conditions. Validating phosphorylation at Ser496 helps unravel context-specific AMPK regulatory mechanisms and their physiological relevance.