Anti-NFKB2

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Nuclear Factor Kappa-B, Subunit 2, also known as NFKB or p52/p100 subunit, is a protein that in humans is encoded by the NFKB2 gene. Liptay et al.(1992) mapped the gene for what they called the p49/p100 subunit of NFKB to chromosome 10 by Southern blot analysis of panels of human/Chinese hamster cell hybrids. By fluorescence in situ hybridization(FISH), they confirmed the localization and mapped the gene with greater resolution to 10q24. NFKB2 appears to be the same as LYT10. Claudio et al.(2002) showed that bone marrow(BM) cells from Nfkb2-deficient mice, but not Nfkb1-deficient mice, failed to increase relative and total IgD-positive transitional-1(T1) stage B cells in response to Baff. In vivo, however, Nfkb2-deficient mice did generate mature B cells, but at reduced numbers. Mice of the aly/aly strain, which are naturally deficient in Nik, and mice of the A/WySNJ strain, which have a mutation in Baffr, also failed to produce T1 B cells in response to Baff. Baff stimulation enhanced expression of Bcl2 in T1 B cells, thereby promoting B-cell survival, and caused the processing of the p100 form of the protein to p52, which again required Baffr and Nik, but not Nemo(IKKG). Immunoblot analysis showed that BM cells contained primarily p100. Protein function: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF- kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14- activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form, the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. [The UniProt Consortium]