Recombinant Human Serine/threonine-protein kinase SIK3 (EC 2.7.11.1) fragment (amino acids 60-388) is a high-purity protein designed for studying the specific functions of its contained Protein kinase and UBA domains. This fragment serves as an essential tool for researchers investigating mTOR signaling regulation, cAMP pathway modulation, and related cellular processes.

The full-length Serine/threonine-protein kinase SIK3 is a crucial regulator of mTOR signaling that promotes the degradation of DEPTOR, a known mTOR inhibitor. This kinase plays a significant role in chondrocyte differentiation during skeletogenesis and negatively regulates the cAMP signaling pathway, potentially through its actions on CRTC2/TORC2 and CRTC3/TORC3. SIK3 also prevents HDAC4 nuclear translocation and localizes to cytoplasmic punctate structures when bound to YWHAZ. These functions highlight SIK3's importance in key signaling pathways and cellular differentiation processes.