NF-κB p65 Rabbit Polyclonal Antibody (ER0815)

UNIPROT #

Q04206

PROTEIN NAME

NF-κB p65

SYNONYMS

Avian reticuloendotheliosis viral (v rel) oncogene homolog A antibody;MGC131774 antibody;NF kappa B p65delta3 antibody;NFKB3 antibody;Nuclear Factor NF Kappa B p65 Subunit antibody;Nuclear factor NF-kappa-B p65 subunit antibody;Nuclear factor of kappa light polypeptide gene enhancer in B cells 3 antibody;Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3 antibody;OTTHUMP00000233473 antibody;OTTHUMP00000233474 antibody;OTTHUMP00000233475 antibody;OTTHUMP00000233476 antibody;OTTHUMP00000233900 antibody;p65 antibody;p65 NF kappaB antibody;p65 NFkB antibody;relA antibody;TF65_HUMAN antibody;Transcription factor p65 antibody;v rel avian reticuloendotheliosis viral oncogene homolog A (nuclear factor of kappa light polypeptide gene enhancer in B cells 3 (p65)) antibody;V rel avian reticuloendotheliosis viral oncogene homolog A antibody;v rel reticuloendotheliosis viral oncogene homolog A (avian) antibody;V rel reticuloendotheliosis viral oncogene homolog A, nuclear factor of kappa light polypeptide gene enhancer in B cells 3, p65 antibody;NF-κB p65;NF κB p65;NF-κB p65

POST-TRANSLATIONAL MODIFICATION

Ubiquitinated by RNF182, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response.; Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity).; Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity). Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.; Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2.; S-nitrosylation of Cys-38 inactivates the enzyme activity.; Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.; Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.; Proteolytically cleaved within a conserved N-terminus region required for base-specific contact with DNA in a CPEN1-mediated manner, and hence inhibits NF-kappa-B transcriptional activity.

SUBCELLULAR LOCATION

Nucleus, cytoplasm.

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. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins. NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression.