- CITATIONS: 2
|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 phospho-peptide corresponding to residues surrounding serine 486 of human NF-kappa-B protein. This antibody detects both phosphorylated and non-phosphorylated version of human NF-kappa-B protein|
|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-kappa-B p65 Antibody 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). A phosphorylation at serine 468 of NF-B by GSK3 beta and IKK beta has been linked negative regulation of NF-B without the inhibition of NF-B nuclear translocation after TNF-alpha or IL-1 beta stimulation (5).
1. Baldwin, A. S., Jr. Annu. Rev. Immunol. 14, 649-683, 1996.
2. Verma, I., et al. Genes Dev. 9, 2723-2735, 1995.
3. Schmitz, M., et al. J. Biol. Chem. 270, 15576-15584. 1995.
4. Marc D. Jacobs Stephen C. Harrison, Cell. 95(6):749-758, 1998.
5. Schwabe, R.F. Sakurai, H. FASEB J Jul 26 epub, 2005.
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