Recombinant SIK1 protein (His tag)

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Recombinant Human Serine/threonine-protein kinase SIK1 (EC 2.7.11.1) Fragment (residues 1-352) – a high-purity protein encompassing the complete Protein kinase and UBA domains, ideal for investigating kinase activity, substrate interactions, and regulatory mechanisms in cellular signaling pathways.

Serine/threonine-protein kinase SIK1 is a multifunctional enzyme involved in critical cellular processes including cell cycle regulation, gluconeogenesis, lipogenesis, muscle differentiation, and tumor suppression. It phosphorylates key targets such as HDAC4, HDAC5, PPME1, SREBF1, and CRTC1/TORC1, thereby modulating CREB activity, p53-dependent anoikis, sodium-sensing networks, and circadian clock entrainment. SIK1 acts as a tumor suppressor by promoting apoptosis upon cell detachment and regulates metabolic pathways through coactivator inhibition. The protein localizes to both the cytoplasm and nucleus, with cytoplasmic retention observed when inactive due to cAMP-induced phosphorylation. This recombinant fragment (1-352) retains the functional kinase and UBA domains, enabling focused studies on SIK1's catalytic and binding properties.