Phospho-SAPK/JNK (Thr183/Tyr185) Recombinant Rabbit mAb (S-3537)

Phospho-SAPK/JNK (Thr183/Tyr185) refers to the activated form of Stress-Activated Protein Kinase/c-Jun N-terminal Kinase (SAPK/JNK) that is simultaneously phosphorylated at its threonine 183 (Thr183) and tyrosine 185 (Tyr185) residues. As a key member of the Mitogen-Activated Protein Kinase (MAPK) family, it is primarily activated by environmental stress signals such as ultraviolet radiation, gamma rays, inflammatory cytokines, and oxidative stress. Its activation depends on the dual phosphorylation of these two critical residues, Thr183 and Tyr185, by upstream kinases MKK4 or MKK7. This modification acts like a "molecular switch," altering JNK's conformation from an inactive to an active state. Once activated, Phospho-SAPK/JNK (Thr183/Tyr185) dimerizes and translocates into the nucleus. Inside the nucleus, it phosphorylates transcription factors like c-Jun and ATF-2, thereby regulating the expression of a suite of genes involved in cellular stress response, apoptosis, inflammation, and even proliferation and differentiation. Consequently, this specific phosphorylated form of the protein is not only a direct marker for JNK pathway activation, but its dysregulated activity is also closely linked to various pathological processes, including neurodegenerative diseases, inflammatory conditions, and cancer, making it a significant target in life science research and the exploration of disease mechanisms.