Activation of NF-Kappa B via Coordination of cIAP, TRAF and Kinase NIK

Thu, 03/11/2010 - 11:56

Recent antibody studies have suggested that nuclear factor κB-inducing kinase (NIK) is inhibited through proteasome-controlled degradation regulated by TRAF/cIAP proteins. cIAP1 and cIAP2 are fairly recent apoptosis inhibitors and represent some of the newer products in our antibody catalog.

NF-kB (nuclear factor kappa-light-chain-enhancer of activated B cells) is found in practically all mammalian cells and is a transcriptional factor of DNA. It affects the cellular response to a range of stimuli, including free radicals, UV radiation and stress. It plays an important role in the immune response to pathogens, but disruption of the regulatory pathways can lead to cancer and other diseases.

The TNF receptor-associated factor (TRAF) family are adaptor proteins which link various cell receptors to MAPK signaling cascades, thus activating NF-kB. TRAF proteins are important transducers for the TNF and the IL-1/TLR receptor complexes. They play an important role in the adaptive and innate immune responses.

The C-terminals of TRAF2 and TRAF3 interact with receptor domains following ligand-induced oligomerization. They interact with a number of pro and anti-apoptosis proteins, meaning TRAF signaling can promote either cell death or survival. The cell signaling proteins in our antibody catalog are used for both pro and anti-apoptosis studies in both healthy and cancerous cells.

Recent IHC assays showed that NIK degradation was dependent on a TRAF3/NIK, TRAF2/cIAP1 and TRAF2/cIAP2 regulatory complex. cIAP1 and cIAP2 appeared to play redundant roles in NIK degradation, as deactivation of both proteins was required for non-canonical NF-kB activation and B-lymphocyte survival. The NIK pathway is tightly regulated, meaning a single gene is enough to reverse lethal TRAF deficiency.

Our antibody catalog at Novus Biologicals is constantly being updated to reflect new signaling pathway findings.


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