TBK1 (pS172) Mouse, PE, Clone: J133-587, BD

Description

• NF-κB is a ubiquitously expressed transcription factor that regulates many cytokine and Ig genes
• It is involved in immune, inflammatory, viral, and acute phase responses
• In most cells, NF-κB is sequestered in an inactive cytoplasmic form via interactions with the inhibitory proteins IκBα, IκBβ, and IκBε
• Stimulation induces the release, activation, and nuclear translocation of NF-κB
• Release of NF-κB results from the phosphorylation and proteolytic degradation of the IκB proteins
• Two cytokine-inducible IκB kinases (IKKα and IKKβ) phosphorylate and target the IκB proteins for degradation via the ubiquitin pathway
• IKKγ/NEMO, a third member of the IKK complex, functions as a regulatory subunit and interacts directly with IKKβ
• TBK1 (TANK-binding kinase 1, also known as T2K or NAK), a protein of 729 amino acids, is another member of the IKK family of kinases regulating NF-κB downstream of the tumor necrosis factor and Toll-like receptor pathways
• TBK1 forms a complex with the adaptor proteins TANK (TRAF-associated NF-κB activator) and TRAF2 (TNF-receptor-associated factor 2), and this oligomer is required for activation and phosphorylation of TBK1 at serine 172 (S172)
• The J133-587 monoclonal antibody recognizes the phosphorylated S172 of human TBK1
• Our in-house testing is performed on a cell line that has been co-transfected with TBK1 and IRF-7 because we have been unable to detect endogenous TBK1 (pS172) by western blotting of lysates from activated cell lines (HeLa activated with PMA and A431 activated with PDGF)
• In the transfectants, the over-expression of TBK1 is necessary for phosphorylation of IRF-7, but the presence of IRF-7 does not affect TBK1 expression or phosphorylation
• We confirmed that mAb J133-587 does not cross-react with IRF-7 by ELISA
• Intracellular Staining