|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||105356 Da|
|Other Names||Nuclear factor NF-kappa-B p105 subunit, DNA-binding factor KBF1, EBP-1, Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1, Nuclear factor NF-kappa-B p50 subunit, NFKB1|
|Target/Specificity||A synthetic peptide corresponding to residues in the nuclear factor NF-κB p50 subunit was used as immunogen. This antibody will detect both forms; p50 and p105.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NF-κB Antibody (p105/p50) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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 and the heterodimeric p65-p50 complex appears to be most abundant one. 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. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 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. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.|
|Cellular Location||Nucleus. Cytoplasm. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B)|
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Provided below are standard protocols that you may find useful for product applications.
Nuclear factor B (NF-B) encompasses an important family of inducible transcriptional activators that regulate a wide variety of cellular and viral genes (1). The family members include p50, p52, p65 (RelA), c-Rel, and RelB (2). Association with inhibitory proteins of the IκB family retains NF-κB in the cytoplasm. Degradation of IB proteins exposes the nuclear localization sequence (NLS), leading to nuclear translocation and subsequent binding of NF-B to DNA (3). The p105 precursor protein acts as an NFκB inhibitor, retaining Rel subunits in the cytoplasm of unstimulated cells. Upon stimulation by TNFα and IL -1α, degradation of p105 occurs; the Rel subunit is released and translocats to the nucleus (4). Additionally, p105 will be proteolytically processed by the 26S proteasome to produce a smaller, transcriptionally active form (p50) (5).
1. Baldwin , A. S., Jr. (1996) Annu. Rev. Immunol. 14, 649-683
2. Verma, I., Stevenson, J., Schwarz, E., Van Antwerp, D. & Miyamoto, S. (1995) Genes Dev. 9, 2723-2735
3. Marc D. Jacobs Stephen C. Harrison. (1998); Cell Volume 95, Issue 6, 749-758
4. Rice, N. R., MacKichan, M. L., and Israel, A. (1992) Cell 71, 243-253
5. Palombella, V. J., Rando, O. J., Goldberg, A. L., and Maniatis, T. (1994) Cell 78, 773-785
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