Anti-NAK/TBK1 Antibody Picoband®

Serine/threonine-protein kinase TBK1, also called TANK-binding kinase 1 or NF-kappa-B-activating kinase is an enzyme that in humans is encoded by the TBK1 gene. The gene was assigned to human chromosome 12q14.2. Serine/threonine kinase plays an essential role in regulating inflammatory responses to foreign agents. TBK1 and NF-kappa-B signaling are essential in KRAS mutant tumors, and established a general approach for the rational identification of codependent pathways in cancer.

Epigenetics and Nuclear Signaling, NFKB Pathway, Nuclear Signaling, Nuclear Signaling Pathways, Protein Phosphorylation, Ser/Thr Kinases, Signal Transduction, Signaling Pathway

Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes. Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus. Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser- 177', thus enhancing LC3 binding affinity and antibacterial autophagy. Phosphorylates and activates AKT1. Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C. Phosphorylates Borna disease virus (BDV) P protein. .

1. Barbie, D. A., Tamayo, P., Boehm, J. S., Kim, S. Y., Moody, S. E., Dunn, I. F., Schinzel, A. C., Sandy, P., Meylan, E., Scholl, C., Frohling, S., Chan, E. M., and 23 others. Systematic RNA interference reveals that oncogenic KRAS-driven cancers require TBK1. Nature 462: 108-112, 2009. 2. Chien, Y., Kim, S., Bumeister, R., Loo, Y.-M., Kwon, S. W., Johnson, C. L., Balakireva, M. G., Romeo, Y., Kopelovich, L., Gale, M., Jr., Yeaman, C., Camonis, J. H., Zhao, Y., White, M. A. RalB GTPase-mediated activation of the I-kappa-B family kinase TBK1 couples innate immune signaling to tumor cell survival. Cell 127: 157-170, 2006. 3. Fingert, J. H., Robin, A. L., Stone, J. L., Roos, B. R., Davis, L. K., Scheetz, T. E., Bennett, S. R., Wassink, T. H., Kwon, Y. H., Alward, W. L. M., Mullins, R. F., Sheffield, V. C., Stone, E. M. Copy number variations on chromosome 12q14 in patients with normal tension glaucoma. Hum. Molec. Genet. 20: 2482-2494, 2011. 4. Fujita, F., Taniguchi, Y., Kato, T., Narita, Y., Furuya, A., Ogawa, T., Sakurai, H., Joh, T., Itoh, M., Delhase, M., Karin, M., Nakanishi, M. Identification of NAP1, a regulatory subunit of I-kappa-B kinase-related kinases that potentiates NF-kappa-B signaling. Molec. Cell. Biol. 23: 7780-7793, 2003.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.