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Fish IRF6 (show IRF6 ELISA Kits) is distinguished from the homolog of mammals by being a positive regulator of IFN transcription and phosphorylated by MyD88 (show MYD88 ELISA Kits) and TBK1, suggesting that differences in the IRF6 (show IRF6 ELISA Kits) regulation pattern exist between lower and higher vertebrates.
TBK1 duplication is found in normal tension and not in high tension open-angle glaucoma patients of Indian origin.
A broader phenotypic range may be associated with TBK1 copy-number variations, although mutations in this gene are most often detected in patients with normal-tension glaucoma.
Autoubiquitination of TRIM26 (show TRIM26 ELISA Kits) links TBK1 to NEMO (show IKBKG ELISA Kits) in RLR (show DHX58 ELISA Kits)-mediated innate antiviral immune response
ALS (show IGFALS ELISA Kits)-linked mutations in OPTN (show OPTN ELISA Kits) and TBK1 can interfere with mitophagy, suggesting that inefficient turnover of damaged mitochondria may represent a key pathophysiological mechanism contributing to neurodegenerative disease.
Mutations in the TBK1 gene were identified to cause amyotrophic lateral sclerosis (ALS)
In combination with phosphorylation of S177 and S513, this posttranslational modification promotes recruitment and retention of OPTN (show OPTN ELISA Kits)/TBK1 on ubiquitinated, damaged mitochondria
TBK1 should thus also be sequenced, after exclusion of C9orf72 mutation, in patients presenting frontotemporal dementia, particularly in cases secondarily associated with amyotrophic lateral sclerosis
TBK1 carriers with amyotrophic lateral sclerosis had shorter disease duration than carriers with frontotemporal dementia in a Belgian cohort.
The expression of TBK1 in mammalian cell mitosis is reported, including localization of the protein during division and its binding properties.
Optineurin (show OPTN ELISA Kits) and TANK-binding kinase 1 (TBK1) are transiently recruited to the polyubiquitinated mitochondria, and the activated TBK1 phosphorylates p62 (show GTF2H1 ELISA Kits) at S403
Innate immune responses to adenovirus vectors are largely TBK1-dependent in the spleen but TBK1-independent in the liver
Data show that the formation of a tripartite ribosomal protein S6 kinase 1 (S6K1 (show RPS6KB1 ELISA Kits))-STING membrane protein-TANK-binding kinase 1 (TBK1) complex was necessary for the activation of interferon regulatory factor-3 (IRF3 (show IRF3 ELISA Kits)).
This study suggest that TBK1 exerts pronociceptive effects in inflammatory nociception which are due to both modulation of NF-kappaB dependent genes and regulation of MAPKs and c-fos.
TRIM27 (show RFP ELISA Kits) inhibits VSV infection-induced type I IFN production by promoting TBK1 degradation.
Suggest that by reducing production of cAMP in adipocytes, PDE3B, IKKepsilon (show IKBKE ELISA Kits) and TBK1 may contribute to the repression of energy expenditure during obesity.
TBK1 has a role in regulating T-cell activation and migration
findings demonstrate a novel regulatory circuit in which STING and TBK1 reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A (show PPM1A ELISA Kits) dephosphorylates STING and TBK1
our results identify CK2 (show CSNK2A1 ELISA Kits) as a novel regulator of TBK1 and IRF3 (show IRF3 ELISA Kits) and suggest that targeting CK2 (show CSNK2A1 ELISA Kits) by small molecular inhibitor may be a viable approach to prevent and treat viral infections.
A role for APPL1 (show APPL1 ELISA Kits) in TLR3 (show TLR3 ELISA Kits)/4-dependent TBK1 and IKKepsilon (show IKBKE ELISA Kits) activation in macrophages.
The results highlight the importance of the C-terminal region in the functional activity of IKKepsilon (show IKBKE ELISA Kits) in innate immune response.Interestingly, corresponding region and residues are not required for activation of downstream signaling by TBK1.
The NF-kappa-B (NFKB) complex of proteins is inhibited by I-kappa-B (IKB) proteins, which inactivate NFKB by trapping it in the cytoplasm. Phosphorylation of serine residues on the IKB proteins by IKB kinases marks them for destruction via the ubiquitination pathway, thereby allowing activation and nuclear translocation of the NFKB complex. The protein encoded by this gene is similar to IKB kinases and can mediate NFKB activation in response to certain growth factors.
serine/threonine-protein kinase TBK1
, TANK-binding kinase 1
, NF-kappa-B-activating kinase
, TANK binding kinase 1
, serine/threonine protein kinase TBK1
, serine/threonine-protein kinase TBK1-like
, NF-kB-activating kinase