NF-κB P65 Antibody #abs130600

abs130600-50ug

In Stock

201

abs130600-100ug

In Stock

301

Description

The formation of the NFKB complex involves the binding of either NFKB1 or NFKB2 to REL, RELA, or RELB. Among these combinations, the p50 (NFKB1)/p65 (RELA) heterodimer is the most prevalent. However, the NFKB complex can be inhibited by I-kappa-B proteins, namely NFKBIA or NFKBIB, which function by trapping NFKB in the cytoplasm. To activate the NFKB complex, I-kappa-B proteins undergo phosphorylation on serine residues by kinases like IKBKA or IKBKB. This phosphorylation process marks the I-kappa-B proteins for degradation via the ubiquitination pathway. Consequently, the NFKB complex is released and becomes active. Once activated, the NFKB complex moves into the nucleus and binds to specific DNA regions known as kappa-B-binding motifs. These motifs are typically represented as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime, where H can be A, C, or T, R can be an A or G purine, and Y can be a C or T pyrimidine.

Other names

RelA, also known as v rel avian reticuloendotheliosis viral oncogene homolog A, is a transcription factor that belongs to the nuclear factor of kappa light polypeptide gene enhancer in B cells 3 (p65) family. It is encoded by the Avian reticuloendotheliosis viral (v rel) oncogene homolog A gene, also known as NFKB3 or MGC131774.
The protein product of RelA, p65 NF kappaB, is a subunit of the nuclear factor NF-kappa-B complex. It plays a crucial role in regulating the expression of genes involved in immune responses, inflammation, cell proliferation, and survival.
RelA is characterized by its ability to bind to specific DNA sequences and activate the transcription of target genes. It interacts with other subunits of the NF-kappa-B complex, forming a heterodimer that translocates into the nucleus and binds to kappa-B sites in the DNA.
Mutations or dysregulation of RelA have been associated with various diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions. Its overactivation has been observed in many cancers, where it promotes tumor growth, angiogenesis, and metastasis.
Understanding the function and regulation of RelA is essential for developing targeted therapies against diseases involving dysregulated NF-kappa-B signaling. Further research is needed to elucidate the complex mechanisms through which RelA influences gene expression and cellular responses.

Source

Rabbit

Specificity

The NF-κB p65 Antibody is designed to specifically target and detect NF-κB p65 at its naturally occurring levels in the body. By utilizing this antibody, researchers can accurately identify and study the endogenous expression of NF-κB p65. This antibody provides a powerful tool to investigate the functional role of NF-κB p65 in various biological processes.

Species Reactivity

Human;Mouse

Application

The dilution ranges for WB are 1:500-1:2000, for IHC are 1:50-1:200, for IF/ICC are 1:100-1:500, and for ELISA (peptide) are 1:20000-1:40000. These dilution ranges are crucial for accurately detecting and visualizing target proteins in different assays. It is important to carefully optimize the dilutions to achieve optimal signal-to-noise ratio and to minimize background noise. By using the appropriate dilution, researchers can ensure reliable and reproducible results in their experiments.

Immunogen

NF-κB p65, a human-derived protein, serves as the basis for a synthesized peptide. The objective is to create a new content while retaining the key information from the original text.

Properties

Concentration

1mg/ml

Purification

We employed SulfoLink™ Coupling Resin for peptide affinity chromatography to purify the antiserum.

Clonality

Polyclonal Antibody

Stability & Storage

Store at -20 °C for one year. Avoid repeated freeze/thaw cycles

Storage buffer

Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.

Target

Background

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).

Posttranslational modification

Ubiquitinated, 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 (PubMed:18212740).

Celluar localization

Cytosol;Nucleus;

UniPort

Q04206