- CITATIONS: 1
|Application ||WB, IHC, IF|
|Calculated MW||60219 Da|
|Other Names||Transcription factor p65, Nuclear factor NF-kappa-B p65 subunit, Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3, RELA, NFKB3|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-terminus of human nuclear factor NF-kappa-B p65 subunit was used as immunogen.|
|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-kappaB Antibody (p65 subunit) 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 p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681).|
|Cellular Location||Nucleus. Cytoplasm. Note=Colocalized with DDX1 in the nucleus upon TNF-alpha induction (By similarity) Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalizes with GFI1 in the nucleus after LPS stimulation.|
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). The p65 subunit, similar to two others in the B family, RelB and c-Rel, contains two transactivation domains in the C-terminal region of the protein (3). Association with inhibitory proteins of the I?B family, retains NF-?B 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 (4). In addition to the nuclear translocation and DNA binding, NF-Bs transcriptional activity is also regulated by coactivators and corepressors in the nucleus. Interaction of p65 with coactivators; CREB-binding protein (Cat # 1496-1 & 1113-1) and p300, increases its transcriptional activity (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. Schmitz, M., dos Santos Silva, M. & Baeuerle, P. (1995) J. Biol. Chem. 270, 15576-15584
4. Marc D. Jacobs Stephen C. Harrison (1198) Cell. Volume 95, Issue 6 , 749-758
5. Gerritsen, M. E., Williams, A. J., Neish, A. S., Moore, S., Shi, Y., and Collins, T. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 2927-2932
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