Phospho-TAK1 (Thr184/187) Recombinant Rabbit mAb (S-4146)

Phospho-TAK1 (Thr184/187) refers to the activated form of transforming growth factor-β-activated kinase 1 (TAK1) that is doubly phosphorylated at threonine residues 184 and 187 within its activation loop. TAK1 is an important member of the mitogen-activated protein kinase kinase kinase (MAP3K) family and participates in regulating various biological processes, including inflammation, immune responses, and cell differentiation. Upon stimulation by pro-inflammatory cytokines (such as TNF-α or IL-1β) or pathogen-associated molecular patterns, upstream signaling molecules (such as TRAF6 and TAK1-binding proteins) promote the ubiquitination and multimerization of TAK1, thereby inducing phosphorylation at Thr184 and Thr187. This dual phosphorylation at these two sites is a critical event for TAK1 activation, significantly enhancing its kinase activity. Subsequently, TAK1 phosphorylates downstream substrates such as the IKK complex (initiating the NF-κB pathway) and MKKs (activating the JNK and p38 MAPK pathways), thereby coordinating cell survival, apoptosis, and gene expression in response to stress and inflammation. Therefore, detecting the phosphorylation status of Thr184/187 is widely used as a marker to assess TAK1 kinase activity and holds significant importance in research on inflammation, autoimmune diseases, and the tumor microenvironment.