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Details for Product No. ABIN967600

Nuclear Factor-KB P65 (NFkBP65) (pSer536) antibody

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Antigen
Synonyms C-Rel, Xrel2, c-rel, rel-A, v-rel, xrel, zgc:100833, p65, NFkB
Epitope
»Alternatives pSer536
Reactivity
»Alternatives Human
Host
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
Conjugate
»Alternatives Un-conjugated
Application
»Alternatives Western Blotting (WB)
Pubmed 3 references available
Catalog no. ABIN967600
Quantity 0.1 mg
Price
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Immunogen Phosphorylated Human or Mouse NF-kappaB p65 Peptide
Clone J144-460
Isotype IgG1, kappa
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Purity Purified
Alternative Name NF-kappa B p65
Background Nuclear factor kB (NF-kB) is a ubiquitously expressed transcription factor that regulates the expression of 200-300 genes. It is crucial for basic cellular responses to stress and pathogens, such as proliferation, survival, development, and apoptosis. The most studied NF-kB complex consists of the p50 (also known as NF-kB1) and p65 (also known as REL-A) subunits, both containing a 300-amino acid region with homology to the Rel proto-oncogene product (RH domain). The RH domain contains motifs for dimerization, nuclear localization, and binding to specific DNA sequences. In addition to the RH domain, the p65 subunit contains the transactivation domain, which is responsible for the interaction with the inhibitor IkB and which contains phosphorylation sites. In most cell types, the p50/p65 heterodimer is located within the cytoplasm complexed to IkB. This complex prevents nuclear translocation and activity of NF-kB. In response to stimuli such as cytokines, LPS, DNA damage, and viral infections, IkB is phosphorylated at critical residues. This phosphorylation induces dissociation of the IkB/NF-kB complex, allowing the free heterodimeric NF-kB to translocate to the nucleus. Furthermore, optimal activation of NF-kB requires phosphorylation in the transactivation domain of p65. In the nucleus, activated NF-kB dimers bind to the kB sites within promoters and enhancers and function as transcriptional activators. The J144-460 monoclonal antibody recognizes the phosphorylated serine 536 (pS536) in the transactivation domain of human NF-kB p65.
Molecular Weight 65 kDa
Comment

Related Products: ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/ml
Buffer Aqueous buffered solution.
Preservative Sodium azide
Storage 4 °C
Product cited in: Viatour, Merville, Bours et al.: "Phosphorylation of NF-kappaB and IkappaB proteins: implications in cancer and inflammation." in: Trends in biochemical sciences, Vol. 30, Issue 1, pp. 43-52, 2005 (PubMed).

Natoli, Saccani, Bosisio et al.: "Interactions of NF-kappaB with chromatin: the art of being at the right place at the right time." in: Nature immunology, Vol. 6, Issue 5, pp. 439-45, 2005 (PubMed).

Siebenlist, Brown, Claudio: "Control of lymphocyte development by nuclear factor-kappaB." in: Nature reviews. Immunology, Vol. 5, Issue 6, pp. 435-45, 2005 (PubMed).

Alternatives for antigen "Nuclear Factor-KB P65 (NFkBP65)", type "Antibodies"
Hosts (692), (54), (6), (4), (1)
Reactivities (735), (426), (348), (81), (78), (78), (38), (8), (6), (3), (2), (2), (2), (2), (2), (1)
Applications (554), (267), (248), (189), (111), (104), (100), (31), (17), (14), (13), (7), (5), (4), (3), (2), (2), (1)
Conjugates (16), (11), (10), (10), (10), (10), (10), (10), (10), (10), (10), (2), (1), (1)
Epitopes (47), (43), (43), (42), (31), (31), (29), (28), (27), (22), (18), (15), (12), (7), (6), (6), (6), (4), (4), (4), (4), (3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
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