|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 536 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 Phospho (pS536) 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.|
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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). 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 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 (4). p65 phosphorylation events occur in the cytoplasm or in the nucleus and are stimuli-specific and cell-type specific, on serine 276, 529, and 536 by various kinases, such as PKA, casein kinase II, IKK beta, and RSK1. Phosphorylation on these sites has been linked to regulation of NF-κB activation (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. Wang, Y, et al., Br J Pharmacol. 2006 July; 148(6): 814
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