ELISA, Immunohistochemistry, Western Blot. This affinity purified antibody has been tested for use in ELISA, immunohistochemistry and western blotting. Specific conditions for reactivity should be optimized by the end user. By western blot, a band approximately 65 kDa in size corresponding to phosphorylated p65 (RelA) protein is expected in the appropriate cell lysate or extract. This phospho-specific polyclonal antibody reacts with human p65 (RelA) pS536 and shows minimal reactivity by western blot with non-phosphorylated p65 (RelA) and minimal reactivity by ELISA against the non-phosphorylated form of the immunizing peptide.
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Description
This product was affinity purified from monospecific antiserum by immunoaffinity chromatography using phospho-peptide coupled to agarose beads followed by solid phase adsorption against nonphospho-peptide. This antibody is specific for human p65 (RelA) protein phosphorylated at S536. A BLAST analysis was used to suggest cross reactivity with p65 (RelA) from human, mouse and rat based on 100% homology with the immunizing sequence. Cross reactivity with p65 (RelA) from other sources has not been determined.
Immunogen
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to a c-terminal region near phospho Serine S536 of human p65 (RelA) protein.
Manna SK, Aggarwal RS, Sethi G, et al. Morin (3,5,7,2',4'-Pentahydroxyflavone) abolishes nuclear factor-kappaB activation induced by various carcinogens and inflammatory stimuli, leading to suppression of nuclear factor-kappaB-regulated gene expression and up-regulation of apoptosis. Clin. Cancer Res. 2007 Apr 1;13(7):2290-2297.