NF-kB p65 Antibody | Affinity Biosciences

$FIGURE 5 | Feline and human BCA2 restrict HIV-1 transcription by preventing HIV-1-induced activation of NF-κB.. (B,C) Five million HEK293T cells were transfected with 5 µg of VR1012, hBCA2, fBCA2, hBCA2 CA, or fBCA2 CA. After 48 h, cytoplasmic and nuclear fractions were separated and analyzed by western blotting to evaluate NF-κB 1(p105/p50), NF-κB p65, BCA2, GAPDH, and Histone H3 in each fraction. Results of quantitative band scan analysis of NF-κB p50/p65 were shown below, and the percentage of VR1012 quantifications are set to 100%.$

FIGURE 5 | Feline and human BCA2 restrict HIV-1 transcription by preventing HIV-1-induced activation of NF-κB.

Fig.

FIGURE 2|Byakangelicin alleviates liver injury in a carbon tetrachloride-induced model.

Fig.

Figure 6.

Fig.

Figure 6 Western blot analysis revealed that the silencing of MyD88 markedly inhibited the expression NF-κB (p65), p-NF-κB (p-p65), AP-1 (c-jun) and p-AP-1 (p-c-jun) protein in the SW480 and HCT116 cells.

FIGURE 7 NF-κB/TWIST1 mediates the effect of S.

FIGURE 4 The deficiency of Smad4 inhibited the inflammatory response in a cellular model of human insulin resistance.

Figure 3 THP-1-derived macrophages regulate Ang1 and NF-κB pathways in HUVECs.

Figure 10.

FIGURE 8 Effects of OCOP and COP on the NF-κB pathway in DSS-induced mice (A) Representative Western blotting images of pIκBα, IκBα, cytoplasmic p65 and nuclear p65 (B–E) The protein expression levels of pIκBα, IκBα, cytoplasmic p65 and nuclear p65 in the NF-κB pathway.

Figure 3 Treatment with HP promotes apoptosis of Dami cells through the NF-κB/IL-17 pathway.

FIGURE 6 The protein levels of Dectin1, TLR2, TLR4, and their associated downstream effector NF-κBp65 are declined post sodium houttuyfonate (SH) management.

Fig.

Figure 3 Nampt promoted LPS-induced inflammation in MC3T3-E1 cells.

Figure 5 Tumor necrosis factor-induced protein-8 (TIPE)-mediated activation of the PI3K/Akt pathway is involved in the modulation of DcR3 levels in HCT116 cells.

Figure 8 Inhibition of TLR4/MAPK/NF-κB signaling pathway.

Figure 6: |MEL attenuated the protein levels of NLRP3, TLR4, NF-κB, and caspase-1 of the terminal ileum tissues in NEC mice.

Fig.

FIGURE 5 Effects of POL, ACT, and FTB on Keap1-Nrf2 and NF-κB p65 signaling pathways in TNF-α-induced cell injury in A549 cells (A,B) Western blot analyses of nucl-Nrf2, cyto-Nrf2, Keap1, nucl-p65, cyto-p65, and p-IκBα (C–F) Intensity of Keap1, cyto-Nrf2, p-IκBα, and cyto-p65 relative to β-actin.

Figure 5 Effect of TOLLIP knockdown and overexpression on the PQ-induced activation of NLRP3 inflammasome in HK-2 cells.

FIGURE 3 Effect of DPSC‐Exos on the expression of TLR4, MyD88, NF‐κB p65 and HMGB1 on day 7 after cerebral I/R damage.

Figure 6 BE-BJO inhibited the activation of the NF-κB signaling pathway.

Figure 5.

Fig.

FIGURE 9 Effects of SAL on the NF-κB signaling pathway.

Fig.

Figure 4.

Figure 6 |C-PC treatment suppresses the expression of NLRP3 inflammasome and NF-κB signaling pathway in lung tissues.

FIGURE 2 | Effects of the RvE1 and LXA4 combination on NF-κB modification.

FIGURE 2 Nicotine aggravates inflammation, oxidative stress and endoplasmic reticulum stress of cochlear hair cells.

Figure 4 miR-155-5p activates the NF-κB signaling pathway in IFN-γ-treated SGECs.

Fig.

Figure 4 Effects of Y-1 and Y-2 on NRK-52e cells’ inflammatory cytokines stimulated by sodium oleate with/without CD36 silences representative.

FIGURE 4| The deficiency of Smad4 inhibited the inflammatory response in a cellular model of human insulin resistance.

FIGURE 9 Effects of PAR-1 knockdown on p-NF-κB p65 by western blot (a) as well as NF-κB p65 (b) and p-NF-κB p65 (c) by immunofluorescence in SH-SY5Y cells treated with high glucose.

Figure 10 RBFOX1 affects the NF-κB and NRF2/HO-1 pathway in H/R-induced HK-2 cells.

Fig.

Figure 5.

Fig.

Figure 4 Effect of MG activated CAP-SIRT1 pathway on NF-κB-mediated inflammatory response in rat macrophages.

Fig.

$FIGURE 5 | Feline and human BCA2 restrict HIV-1 transcription by preventing HIV-1-induced activation of NF-κB. (A) HEK293T cells were co-transfected with 250 ng different variants of BCA2 along with 250 ng of pNF-κB-Luc reporter plasmid and 1 µg of pNL43. After 48 h, the cells were lysed and analyzed for luciferase activity and by western blotting with anti-Flag, and anti-tubulin antibodies. (B,C) Five million HEK293T cells were transfected with 5 µg of VR1012, hBCA2, fBCA2, hBCA2 CA, or fBCA2 CA. After 48 h, cytoplasmic and nuclear fractions were separated and analyzed by western blotting to evaluate NF-κB 1(p105/p50), NF-κB p65, BCA2, GAPDH, and Histone H3 in each fraction. Results of quantitative band scan analysis of NF-κB p50/p65 were shown below, and the percentage of VR1012 quantifications are set to 100%. (D) HEK293T cells were co-transfected with 1 µg of pNL43, 500 ng of hBCA2-Flag, fBCA2-Flag, or VR1012, and the levels of nef RNA were analyzed at 10, 22, and 28 h by RT-qPCR after transfection, and the cell lysates were analyzed by western blotting with anti-Flag, and anti-tubulin antibodies. (E) HEK293T cells were co-transfected with 1 µg of pNL43, 500 ng of different variants of BCA2 or VR1012, and the levels of nef RNA were analyzed 48 h later by RT-qPCR, and the cell lysates were analyzed by western blotting with anti-Flag, and anti-tubulin antibodies. The data were presented as the means ± SDs for three independent experiments. Statistical significance was analyzed by using Student’s t-test. Significant differences are indicated as follows: *P < 0.05; **P < 0.01.$

FIGURE 5 | Feline and human BCA2 restrict HIV-1 transcription by preventing HIV-1-induced activation of NF-κB.

Figure 7 Effects of BJXZ pills on liver p65, P-p65, Nrf2, and HO-1 expression in rats with hepatic fibrosis.

FIGURE 7 Spinal cord nuclear factor‐kappa B (NF‐κB) translocation from the cytoplasm to the nucleus induced by bone cancer pain (BCP).

Figure 5 WKYMVm inhibited the ERK1/2 and NF-κB p65 signaling pathways and affected the p38 signaling pathway in microglial cells.

Fig.

Figure 6 NF-κB nuclear transfer decreased in the mouse kidney.

Fig.

FIGURE 6 Transplantation of FG‐4592 preconditioned bone marrow stromal cell (BMSCs) inhibits microglial activation and inflammation.

Figure 5.

FIGURE 4 Cytoplasmic mtDNA markedly activated STING signalling.

Figure 4 Immunohistochemical staining of TLR4 (a), NF-κB (b), Bax (c), and Bcl-2 (d) and semiquantitative analysis of these proteins expression (e) in intestinal tissues of mice.

Fig.

FIGURE 7 Nesfatin‐1 prevented activation of NF‐κB signaling in SCI mice.

Figure 9 Nrf2 overexpression in vitro promotes PPARγ but inhibits NF-κB nuclear translocation; n = 3 experiments per group.

Figure 5 The expression degrees of HMGB1, TLR4, NF-κB, p-38 MAPK, and ERK1/2 proteins (x¯ ±s).

Figure 7 The effect of OBB on the TLR4/NF-κB signaling pathway in 5-FU-induced IM mice.

Figure 7 XFZYD inhibited the IKBα/NF-κB signaling in rat models with CPB-induced ALI.

Figure 6 BA changed the levels of NF-κB, TLR2, and MYD88 in the lung tissue of COPD rats by immunohistochemical staining and semiquantitative analysis (×100).

Figure 7 BA improved the expressions of MYD88, p–NF–κBp65/NF-κBp65, p-IκBa/IκBa, TLR2, and TLR4 in rat lung tissue.

Figure 4 mRNA and protein expression in knee joint and spleen of CIA rats.

Fig.

Figure 4 The BGF effects on levels of oxidative stress-related factors and inflammasome factors.

Figure 4: Changes of IL-1β, IL-6, NF-kB and YY1- mRNA expression in Frontal cortex (A-D), Striatum (E-H), hippocampus (I-L) among CTR (n = 8), CUMS (n = 8) and VOR group (n = 8); (M) Representative western blot image of NF-kB in nuclear level and cytosolic in the hippocampus among CTR, CUMS and VOR groups;.

Figure 4 The effects of SD treatment on the levels of the TLR4/TRAF6/NF-κB and IL-6/ROR-γt/STAT3 pathways' related genes and proteins in the nasal mucosa of AR mice ((n) = 6).

Figure 6.

Fig.

$Fig. 4. Effects of stigmasterol treatment on inflammatory pathways in Aβ42 oligomers induced BV2 cells. Cells were pretreated with Aβ42 oligomers (1 μM) for 24 h, followed by treatment with stigmasterol (10, 20 μM) for 4 h. (A, B) Representative western blot analysis of AMPK signaling. GAPDH immunoreactivity was used as a loading control. (C-G) Representative western blot analysis of NF-κB signaling. The cytosolic fractions were prepared and analyzed with phosphorylated IκBα, total IκBα, and total NF-κB p65. The nuclear fractions were prepared and analyzed with total NF-κB p65. α-Tubulin immunoreactivity was used as a loading control in the cytosolic fraction, Histone H3 was used as the loading control in the nuclear fraction. (H-K) Representative western blot analysis of NLRP3 signaling, including NLRP3, Caspase-1, and Caspase-1, p20. GAPDH immunoreactivity was used as a loading control. Data were presented as the mean ± SEM from three independent experiments. One-way ANOVA with Tukey’s multiple comparison test revealed a difference between groups.$

Fig.

Figure 5 Effect of MALT1 mucosa-associated lymphoid tissue lymphoma translocation protein 1 on nuclear factor-κB signaling in proatherogenic VSMCs.

FIGURE 6 Cinacalcet suppresses the PKCδ/ERK/P65 signaling pathway.

FIGURE 6 Effect of MLG on NF-κB/Nrf2/HO-1 signaling pathway in ethanol-induced gastric lesions mice.

FIGURE 3 STIP1 ameliorates ischaemia/reperfusion-induced inflammation in rat spinal cord.

FIGURE 4 STIP1 restrains OGD-induced inflammation in microglial cells.

Figure 7 SHFM1 regulates the NF-κB signaling pathway in ESCC cells.

Figure 5 Relative expression levels of NF-κB pathway-related proteins were measured via western blot assay.

Fig.

Figure 6 Effect of DOFE on TLR4-mediated inflammatory response.

Figure 2 The changes in the expression of key proteins of NF-κB and MAPK signaling pathway after LPS stimulation in RECs at different times.

Figure 10.

Figure 4.

Fig.

Figure 6 BMP8B triggers NF-κB signaling to suppress adipogenesis.

Fig.

Figure 7 Effects of adding sanguinarine to a high-fat diet on NF-κB gene expression and protein expression of grass carp.

Figure 4 Effects of AdipoRon on p65 and adenosine monophosphate-activated protein kinase (AMPK) phosphorylation under proinflammatory conditions.

Fig.

Figure 8 Western blot analysis of the proteins.

Fig 3 HEX enhances barrier integrity and limits the NF-κB signaling pathway in MMECs.

Fig.

Figure 9.

Fig.

Figure 4 High-dose VC attenuated the inflammatory response in CLP-induced sepsis rats at 1d, 3d and 5d.

Fig.

Figure 6 Luteolin inhibits the activity of the AGE-RAGE signaling pathway.

Fig.

$Figure 2. ASFV A528R inhibits the NF-κB p65 phosphorylation downstream TLR8 signaling. (A) 293T cells grown in 12-well plate (3 × 105 cells/well) were transfected with A528R plasmid (0.25 µg, 0.5 µg), pTLR8 (0.5 µg) as indicated. Twenty-four hours post transfection, cells were stimulated with R848 (5 µg/mL) for 12 h, the expressions of p-p65, p65, A528R, and pTLR8 were analyzed by Western blotting. (B–D) 293T cells were transfected with A528R (0.25 µg, 0.5 µg) or vector (EV) control (0.5 µg), together with MyD88 (0.5 µg) (B), IKK-β (0.5 µg) (C), p65 (0.5 µg) (D). Twenty-four hours later, the expressions of p-p65, p65, A528R, MyD88, IKK-β, p65 were analyzed by Western blotting. (E) 293T cells grown in 12-well plate (3 × 105 cells/well) were transfected with A528R (0.25 µg, 0.5 µg), pTLR8 (0.5 µg). Twenty-four hours post transfection, cells were stimulated with R848 (5 µg/mL) for 12 h. Cell lysates were fractionated into cytoplasmic and nuclear extracts, and the protein levels of p65 and p-p65 in different fractions were analyzed by Western blotting. The histone-H3 and GAPDH were also shown as the nuclear and cytoplasmic markers, respectively.$

Figure 2.

Figure 7 Pretreatment with CH223191 eliminated the blocking effect of 5-HIAA on NF-κB signaling pathway The expression levels of representative proteins of the NF-κB pathway in mammary (A) and colonic (D) tissues were determined in three groups of mice.

Figure 5.

Fig.

製品:	NF-kB p65 Antibody
カタログ:	AF5006
タンパク質の説明:	Rabbit polyclonal antibody to NF-kB p65
アプリケーション:	WB IHC IF/ICC
反応性:	Human, Mouse, Rat, Monkey
予測:	Pig, Bovine, Horse, Sheep, Dog
分子量:	65~80kDa; 60kD(Calculated).
ユニプロット:	Q04206
RRID:	AB_2834847

類似製品を見る>>

サイズ	価格	在庫状況
100ul	$280	在庫あり
200ul	$350	在庫あり

MSDS

説明書

COA

プロトコル

WB Handbook

IHC Protocol

IF/ICC Protocol

製品説明

ソース:

Rabbit

アプリケーション:

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

反応性:

Human,Mouse,Rat,Monkey

予測:

Pig(100%), Bovine(91%), Horse(91%), Sheep(91%), Dog(100%)

クローナリティ:

Polyclonal

特異性:

NF-kB p65 Antibody detects endogenous levels of total NF-kB p65.

RRID:

AB_2834847
引用形式: Affinity Biosciences Cat# AF5006, RRID:AB_2834847.

コンジュゲート:

Unconjugated.

精製:

The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).

保存:

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.

別名:

折りたたみ／展開

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

免疫原

免疫原:

Uniprot:

Q04206(TF65_HUMAN) >>Visit HPA database.

遺伝子(ID):

RELA(5970)

タンパク質の説明:

NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA, or RELB (MIM 604758) to form the NFKB complex. The p50 (NFKB1)/p65 (RELA) heterodimer is the most abundant form of NFKB. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008 or NFKBIB, MIM 604495), which inactivate NFKB by trapping it in the cytoplasm.

タンパク質配列:

Q04206 TF65_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS

種類予測

種類予測:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species

Results

Score

Pig

100

Dog

100

Horse

Bovine

Sheep

Xenopus

Zebrafish

Chicken

Rabbit

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q04206 基板として

Q04206

Site	PTM Type	Enzyme	Source
M1	Acetylation		Uniprot
K37	Methylation		Uniprot
K37	Sumoylation		Uniprot
C38	S-Nitrosylation		Uniprot
S42	Phosphorylation		Uniprot
S45	Phosphorylation		Uniprot
K56	Ubiquitination		Uniprot
K62	Ubiquitination		Uniprot
T71	Phosphorylation		Uniprot
S75	Phosphorylation		Uniprot
K79	Ubiquitination		Uniprot
K93	Ubiquitination		Uniprot
S112	Phosphorylation		Uniprot
K122	Acetylation		Uniprot
K122	Ubiquitination		Uniprot
K123	Acetylation		Uniprot
K123	Ubiquitination		Uniprot
S131	Phosphorylation		Uniprot
T136	Phosphorylation		Uniprot
R174	Methylation		Uniprot
S180	Phosphorylation		Uniprot
R187	Methylation		Uniprot
K195	Ubiquitination		Uniprot
S205	Phosphorylation		Uniprot
K218	Acetylation		Uniprot
K218	Methylation		Uniprot
K218	Ubiquitination		Uniprot
K221	Acetylation		Uniprot
K221	Methylation		Uniprot
S238	Phosphorylation		Uniprot
S240	Phosphorylation		Uniprot
T254	Phosphorylation		Uniprot
S261	Phosphorylation		Uniprot
S269	Phosphorylation		Uniprot
S276	Phosphorylation	P11309 (PIM1) , O94806 (PRKD3) , O75676 (RPS6KA4) , P17612 (PRKACA) , O75582 (RPS6KA5)	Uniprot
S281	Phosphorylation		Uniprot
T305	O-Glycosylation		Uniprot
T305	Phosphorylation		Uniprot
Y306	Phosphorylation		Uniprot
T308	Phosphorylation		Uniprot
K310	Acetylation		Uniprot
K310	Methylation		Uniprot
K310	Ubiquitination		Uniprot
S311	Phosphorylation	Q05513 (PRKCZ)	Uniprot
K314	Acetylation		Uniprot
K314	Methylation		Uniprot
K314	Ubiquitination		Uniprot
K315	Acetylation		Uniprot
K315	Methylation		Uniprot
K315	Ubiquitination		Uniprot
S316	Phosphorylation	P48729 (CSNK1A1)	Uniprot
S319	O-Glycosylation		Uniprot
T322	O-Glycosylation		Uniprot
S337	O-Glycosylation		Uniprot
S337	Phosphorylation		Uniprot
T352	O-Glycosylation		Uniprot
S374	O-Glycosylation		Uniprot
S374	Phosphorylation		Uniprot
S377	O-Glycosylation		Uniprot
T429	Phosphorylation		Uniprot
T435	Phosphorylation	P28482 (MAPK1)	Uniprot
S468	Phosphorylation	P49841 (GSK3B) , O14920 (IKBKB) , Q14164 (IKBKE)	Uniprot
S472	Phosphorylation		Uniprot
T505	Phosphorylation		Uniprot
S529	Phosphorylation	P68400 (CSNK2A1) , P47710 (CSN1S1)	Uniprot
S536	Phosphorylation	O15111 (CHUK) , O94806 (PRKD3) , Q9Y6K9 (IKBKG) , Q9UHD2 (TBK1) , Q9HCP0 (CSNK1G1) , Q16566 (CAMK4) , P51812 (RPS6KA3) , Q15418 (RPS6KA1) , Q00534 (CDK6) , O14920 (IKBKB) , P24723 (PRKCH) , Q14164 (IKBKE)	Uniprot
S543	Phosphorylation	P68400 (CSNK2A1)	Uniprot
S547	Phosphorylation	Q13315 (ATM)	Uniprot

研究背景

Q04206_TF65_HUMAN

機能:

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. The heterodimeric RELA-NFKB1 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. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. 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. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells. The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression.

PTMs:

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.

細胞の位置付け:

Nucleus. Cytoplasm.
Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B) (PubMed:1493333). Colocalized with DDX1 in the nucleus upon TNF-alpha induction (PubMed:19058135). Colocalizes with GFI1 in the nucleus after LPS stimulation (PubMed:20547752). Translocation to the nucleus is impaired in L.monocytogenes infection (PubMed:20855622).

サブユニット構造:

Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-kappa-B p65-p65 complex. Component of the NF-kappa-B p65-p52 complex. May interact with ETHE1. Binds TLE5 and TLE1. Interacts with TP53BP2. Binds to and is phosphorylated by the activated form of either RPS6KA4 or RPS6KA5. Interacts with ING4 and this interaction may be indirect. Interacts with CARM1, USP48 and UNC5CL. Interacts with IRAK1BP1 (By similarity). Interacts with NFKBID (By similarity). Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB (By similarity). Interacts with NFKBIE. Interacts with NFKBIZ. Interacts with EHMT1 (via ANK repeats) (By similarity). Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14. Interacts with HDAC3; HDAC3 mediates the deacetylation of RELA. Interacts with HDAC1; the interaction requires non-phosphorylated RELA. Interacts with CBP; the interaction requires phosphorylated RELA. Interacts (phosphorylated at 'Thr-254') with PIN1; the interaction inhibits p65 binding to NFKBIA. Interacts with SOCS1. Interacts with UXT. Interacts with MTDH and PHF11. Interacts with ARRB2. Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is part of a SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with DDX1. Interacts with UFL1 and COMMD1. Interacts with BRMS1; this promotes deacetylation of 'Lys-310'. Interacts with NOTCH2 (By similarity). Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation. Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA. Interacts (via the RHD) with GFI1; the interaction, after bacterial lipopolysaccharide (LPS) stimulation, inhibits the transcriptional activity by interfering with the DNA-binding activity to target gene promoter DNA. Interacts (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway. Interacts with MEFV. Interacts with CLOCK (By similarity). Interacts (via N-terminus) with CPEN1; this interaction induces proteolytic cleavage of p65/RELA subunit and inhibition of NF-kappa-B transcriptional activity. Interacts with FOXP3. Interacts with CDK5RAP3; stimulates the interaction of RELA with HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B transcriptional activity. Interacts with DHX9; this interaction is direct and activates NF-kappa-B-mediated transcription. Interacts with LRRC25. Interacts with TBX21 (By similarity). Interacts with KAT2A (By similarity). Interacts with ZBTB7A; involved in the control by RELA of the accessibility of target gene promoters. Directly interacts with DDX3X; this interaction may trap RELA in the cytoplasm, impairing nuclear relocalization upon TNF activating signals.

(Microbial infection) Interacts with human respiratory syncytial virus (HRSV) protein M2-1.

(Microbial infection) Interacts with molluscum contagiosum virus MC132.

(Microbial infection) Interacts with herpes virus 8 virus protein LANA1.

タンパク質ファミリー:

The transcriptional activation domain 3/TA3 does not participate to the direct transcriptional activity of RELA but is involved in the control by RELA of the accessibility of target gene promoters. Mediates interaction with ZBTB7A.

The transcriptional activation domain 1/TA1 and the transcriptional activation domain 2/TA2 have direct transcriptional activation properties (By similarity). The 9aaTAD motif found within the transcriptional activation domain 2 is a conserved motif present in a large number of transcription factors that is required for their transcriptional transactivation activity (PubMed:17467953).

研究領域

· Cellular Processes > Cell growth and death > Apoptosis. (View pathway)

· Cellular Processes > Cell growth and death > Cellular senescence. (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > Ras signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > cAMP signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > TNF signaling pathway. (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > Antifolate resistance.

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Substance dependence > Cocaine addiction.

· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.

· Human Diseases > Infectious diseases: Bacterial > Shigellosis.

· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.

· Human Diseases > Infectious diseases: Bacterial > Pertussis.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Parasitic > Leishmaniasis.

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis C.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Measles.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer. (View pathway)

· Human Diseases > Cancers: Overview > Transcriptional misregulation in cancer.

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

· Human Diseases > Cancers: Specific types > Pancreatic cancer. (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer. (View pathway)

· Human Diseases > Cancers: Specific types > Chronic myeloid leukemia. (View pathway)

· Human Diseases > Cancers: Specific types > Acute myeloid leukemia. (View pathway)

· Human Diseases > Cancers: Specific types > Small cell lung cancer. (View pathway)

· Human Diseases > Immune diseases > Inflammatory bowel disease (IBD).

· Organismal Systems > Immune system > Chemokine signaling pathway. (View pathway)

· Organismal Systems > Aging > Longevity regulating pathway. (View pathway)

· Organismal Systems > Development > Osteoclast differentiation. (View pathway)

· Organismal Systems > Immune system > Toll-like receptor signaling pathway. (View pathway)

· Organismal Systems > Immune system > NOD-like receptor signaling pathway. (View pathway)

· Organismal Systems > Immune system > RIG-I-like receptor signaling pathway. (View pathway)

· Organismal Systems > Immune system > Cytosolic DNA-sensing pathway. (View pathway)

· Organismal Systems > Immune system > IL-17 signaling pathway. (View pathway)

· Organismal Systems > Immune system > Th1 and Th2 cell differentiation. (View pathway)

· Organismal Systems > Immune system > Th17 cell differentiation. (View pathway)

· Organismal Systems > Immune system > T cell receptor signaling pathway. (View pathway)

· Organismal Systems > Immune system > B cell receptor signaling pathway. (View pathway)

· Organismal Systems > Nervous system > Neurotrophin signaling pathway. (View pathway)

· Organismal Systems > Endocrine system > Prolactin signaling pathway. (View pathway)

· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

参考文献

1). An anti-inflammatory and neuroprotective biomimetic nanoplatform for repairing spinal cord injury. Bioactive Materials, 2022 (PubMed: 35845318) [IF=18.9]

Application: WB Species: Mouse Sample:

Fig. 2 Macrophage phenotype regulation based on RA@BSA@Cur NPs. (a) The schematic illustration of RA@BSA@Cur NPs regulated macrophage polarization under LPS. (b) The immunofluorescence and quantification results of RAW264.7 cultured different BSA-related NPs in LPS condition. CD86+ M1 macrophage (yellow arrow) and CD206+ M2 macrophage (white arrow), nuclei (DAPI: blue). Scale bar, 50 μm. (c&d) The flow cytometry analysis and quantification results of RAW264.7 (gated on F4/80+) cultured different BSA-related NPs in LPS condition. (e) The macrophages' M1 inhibition and M2 promotion regulated by RA@BSA@Cur NPs may be through the NF-κB pathway. (f) The inflammatory factors IL-6, TNF-α, and IL-4 changes after RA@BSA@Cur treatment. (n = 3 independent samples). Statistical differences were determined by using the Analysis of Variance (ANOVA) with Bonferroni's multiple comparison test (*p < 0.05, **p < 0.01, ***p < 0.001, ns: no significant; a.u. means arbitrary unit).

2). Opsonization Inveigles Macrophages Engulfing Carrier-Free Bilirubin/JPH203 Nanoparticles to Suppress Inflammation for Osteoarthritis Therapy. Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024 (PubMed: 38593402) [IF=15.1]

3). Upregulation of BCL-2 by acridone derivative through gene promoter i-motif for alleviating liver damage of NAFLD/NASH. NUCLEIC ACIDS RESEARCH, 2020 (PubMed: 32710621) [IF=14.9]

Application: WB Species: mouse Sample: liver

Figure 7. Effect of A22 on ameliorating apoptosis, ER stress, inflammation, metabolic syndrome, and fibrogenesis in HF diet-fed mice. (A) Effect of A22 on BCL-2 gene transcription. (B) Effect of A22 on BAX gene transcription. (C) Effect of A22 on expressions of apoptosis-related proteins in liver. The extracted proteins from the liver were immunoblotted with specific antibodies, and quantified based on the loading control of ACTIN. (D) Effect of A22 on ER stress. The UPR proteins (IRE-1, PERK, elF-2 and CHOP) were analyzed by using western Blot. (E) Effect of A22 on expressions of inflammatory factors. (F) Effect of A22 on expressions of fibrogenic proteins.

4). A novel UV-curable extravascular stent to prevent restenosis of venous grafts. Composites Part B: Engineering, 2021 [IF=13.1]

Application: WB Species: Rat Sample:

Fig. 7. A: Western blot analysis of TLR2/MyD88/NF-κB pathway proteins in venous graft vessels. B: Contents of TLR2/MyD88/NF-κB pathway proteins in venous graft vessels. Data are presented as the mean ± SD; *: compared with control group, p < 0.05. #: compared with sham group, p < 0.05.

5). Phenytoin silver: a new nanocompound for promoting dermal wound healing via comprehensive pharmacological action. Theranostics, 2017 (PubMed: 28255340) [IF=12.4]

Application: IHC Species: human Sample:

Figure 2. PnAg promotes wound healing in SD rats. (A) Photographs of rat skin full-thickness excision wounds on different post-excision days. (B) Change in wound areas of SD rats after treatment; (C) and (D) Expression levels of collagen I, NF-κB, TGF-ß, MMP-2, and MMP-9 in tissues on day 7 and 17 detected by immunohistochemistry. (E) Histogram of protein expression levels in these tissues. (F) and (G) Histomorphological changes in wound tissues stained by Masson trichrome and HE on day 17.

6). YY1 (Yin-Yang 1), a transcription factor regulating systemic inflammation, is involved in cognitive impairment of depression. Psychiatry and Clinical Neurosciences, 2023 (PubMed: 36436207) [IF=11.9]

7). YY1 (Yin‐Yang 1), a transcription factor regulating systemic inflammation is involved in cognitive impairment of depression. Psychiatry and Clinical Neurosciences, 2023 (PubMed: 36436207) [IF=11.9]

8). Arsenic retention in erythrocytes and excessive erythrophagocytosis is related to low selenium status by impaired redox homeostasis. Redox Biology, 2022 (PubMed: 35500533) [IF=11.4]

9). LncRNA AK023391 promotes tumorigenesis and invasion of gastric cancer through activation of the PI3K/Akt signaling pathway. Journal of Experimental & Clinical Cancer Research, 2017 (PubMed: 29282102) [IF=11.3]

Application: WB Species: human Sample: Gastric cancer cells

Fig. 8 | LncRNA AK023391 was involved in the regulation of the PI3K/Akt signaling pathway.e-f Western blotting validation of the effects of AK023391 knockdown on the expression of PI3K/Akt, NF-κB, p53, and FOXO3a pathways, and their downstream transcription factors c-myb, cyclinB1/G2, and BCL-6 in HGC 27, AGS, and SGC-7901 cells

10). YY1 complex promotes Quaking expression via super-enhancer binding during EMT of hepatocellular carcinoma. CANCER RESEARCH, 2019 (PubMed: 30760518) [IF=11.2]

Application: WB Species: human Sample: PLC-PRF-5 cells

Fig. 1 | YY1 is a key transcription factor for QKI expression in PLC-PRF-5 cells. (g) Co-IP of endogenous YY1, p65, and p300 was performed in PLC-PRF-5 cells.

Application: IHC Species: mouse Sample: tumor tissues

Fig. 5| QKI expression is required for the YY1 complex to promote the metastasis and malignancy of HCC. (a) Comparison of PLC-PRF-5 and Hep3B tumor growth in mice were measured starting 6 days after implantation. All of the groups were euthanized on day 24. (b) Metastatic lung nodules were counted in each group. (c) QKI, p65, YY1, E-cadherin, and Vimentin expression levels in the tumor tissues of p65, YY1, p65+YY1, QKI and p65+YY1+siQKI groups analyzed through IHC staining.

Restrictive clause

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.

NF-kB p65 Antibody - #AF5006

関連製品情報

関連ダウンロード

MSDS

説明書

COA

プロトコル

WB Handbook

IHC Protocol

IF/ICC Protocol

製品説明

免疫原

種類予測

PTMs - Q04206 基板として

研究背景

研究領域

参考文献

Restrictive clause