|Other Names||Inhibitor of nuclear factor kappa-B kinase subunit beta, I-kappa-B-kinase beta, IKK-B, IKK-beta, IkBKB, I-kappa-B kinase 2, IKK2, Nuclear factor NF-kappa-B inhibitor kinase beta, NFKBIKB, IKBKB, IKKB|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:30337470). Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation. Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:20410276). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF- dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NCOA3, BCL10 and IRS1 (PubMed:17213322). Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation (PubMed:11297557). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C- terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418).|
|Cellular Location||Cytoplasm. Nucleus. Membrane raft. Note=Colocalized with DPP4 in membrane rafts.|
|Tissue Location||Highly expressed in heart, placenta, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis and peripheral blood|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL(MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form theNFKB complex. The NFKB complex is inhibited by I-kappa-B proteins(NFKBIA, MIM 164008, or NFKBIB, MIM 604495), which inactivateNF-kappa-B by trapping it in the cytoplasm. Phosphorylation ofserine residues on the I-kappa-B proteins by kinases (IKBKA, MIM600664, or IKBKB) marks them for destruction via the ubiquitinationpathway, thereby allowing activation of the NF-kappa-B complex.Activated NFKB complex translocates into the nucleus and binds DNAat kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or Gpurine; and Y is a C or T pyrimidine).
Yatherajam, G., et al. J. Immunol. 185(5):2665-2669(2010)Kenneth, N.S., et al. EMBO J. 29(17):2966-2978(2010)Zhao, M., et al. J. Biol. Chem. 285(32):24372-24380(2010)Niida, M., et al. Mol. Immunol. 47(14):2378-2387(2010)Schuurhof, A., et al. Pediatr. Pulmonol. 45(6):608-613(2010)
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at firstname.lastname@example.org.