TBK1 (human, recombinant)

NAK|NF-κB-Activating Kinase|TANK-Binding Kinase 1

TANK-binding kinase 1 (TBK1) is a non-canonical inhibitor of NF-κB kinase (IKK) that has an essential role in regulating inflammatory responses to pathogens.{35096} Following activation of toll-like receptors by viral DNA, TBK1 interacts with various partners such as STING, MAVS, and TANK to phosphorylate and activate interferon regulatory factors (IRFs) 3 and 7 as well as DEAD-box helicase 3 X-linked (DDX3X), which leads to transcriptional activation of pro-inflammatory and antiviral genes including interferon (IFN) subtypes α and β.{35096,35098} TBK1 induces nuclear translocations of NF-κB to initiate a pro-inflammatory response via phosphorylation of NF-κB inhibitor α (NFκBIα), IKKβ, or NF-κB p65 subunit (RelA).{35099} Cytosolic localization of E. coli, Salmonella, and S. pyogenes increases in TBK1-/- murine embryonic fibroblasts, macrophages, and epithelial cells, suggesting TBK1 maintains vacuolar integrity, which is critical to bacterial clearance.{35095} TBK1 phosphorylates the autophagy receptor optineurin to enhance binding of ubiquitin-like microtubule-associated protein light chain 3 (LC3) modifiers and induce autophagic clearance of S. enterica.{35097} It also binds to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) non-structural protein 13 (Nsp13), a helicase-triphosphatase and a component of the viral replicase-transcriptase complex.{55024} Cayman’s TBK1 (human, recombinant) protein can be used for ELISA, Western blot and enzymatic assays.

-80

-80

50 mM HEPES, pH 8.0, with 150 mM sodium chloride, and 10% glycerol

365

≥50% estimated by SDS-PAGE