The Phospho-p38 (Tyr323) antibody is designed to detect p38 mitogen-activated protein kinase (MAPK) when phosphorylated at tyrosine 323. a regulatory site implicated in its activation or functional modulation. p38 MAPK, part of the conserved MAPK signaling cascade, plays a central role in cellular responses to stress, inflammation, apoptosis, and differentiation. While canonical p38 activation typically involves dual phosphorylation at Thr180 and Tyr182 within the activation loop, phosphorylation at alternative residues, such as Tyr323. may represent isoform-specific or context-dependent regulatory mechanisms. For instance, studies suggest Tyr323 phosphorylation in p38γ (MAPK12) or p38δ (MAPK13) isoforms could influence substrate selectivity or interaction with downstream effectors.
This antibody is widely used in immunoblotting (Western blot), immunofluorescence, or immunoprecipitation to study p38 activation dynamics under physiological or pathological conditions, such as oxidative stress, cytokine stimulation, or disease models (e.g., cancer, neurodegenerative disorders). Researchers must validate its specificity using phosphorylation-blocking peptides or knockout controls, as cross-reactivity with related kinases or non-phosphorylated forms may occur. Optimal results often require fresh lysates treated with phosphatase inhibitors to preserve phosphorylation signals.
Understanding Tyr323 phosphorylation expands insights into p38 regulatory complexity, offering potential therapeutic targets for conditions driven by dysregulated MAPK signaling.