Anti-NF-kB p65/RELA Antibody Picoband® (Dylight488 Conjugate)

RELA (V-REL AVIAN RETICULOENDOTHELIOSIS VIRAL ONCOGENE HOMOLOG A), also called NFKB3 or NFKB, p65 SUBUNIT. NFKB1 or NFKB2 is bound to REL, RELA, or RELB to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins, which inactivate NFKB by trapping it in the cytoplasm. The p65 (RELA) heterodimer is the most abundant form of NFKB. And the RELA gene is located on 11q13.1. RELA is a nonhistone substrate of HDAC3 and that IKBA-dependent nuclear export of the HDAC3-deacetylated RELA replenishes the depleted cytoplasmic pool of latent NFKB-IKBA complexes for subsequent NFKB responses. RELA nucleocytoplasmic redistribution coincided with export of PPARG, and immunoprecipitation analysis indicated that PPARG-RELA association was dependent on the PPARG C-terminal ligand-binding domain. IKK-dependent phosphorylation of RELA on ser468 enhanced binding of GCN5 to RELA and RELA ubiquitination.

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 ly 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). .

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br> Immunohistochemistry (Paraffin-embedded Section), 2-5μg/ml, Human, By Heat <br>Immunocytochemistry/Immunofluorescence , 5μg/ml, Human, -<br>

Nucleus. Cytoplasm. 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. .