Rabbit Anti-RELA Polyclonal Antibody (DPABH-22935)


Host Species
Antibody Isotype
Species Reactivity
Human, Mouse
A synthetic peptide of human RELA


Application Notes
WB:    1:500 - 1:1000; IHC:    1:20 - 1:50; IF:    1:20 - 1:50; FC:    1:20 - 1:50
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Data Examples

Western blot analysis of extracts of various cell lines, using RELA antibody at 1:1000 dilution.Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Basic Kit.Exposure time: 10s.


Alternative Names
RELA; v-rel avian reticuloendotheliosis viral oncogene homolog A; p65; NFKB3; transcription factor p65; NF-kappa-B p65delta3
Entrez Gene ID
UniProt ID


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Custom Antibody Labeling

We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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Study on the Multitarget Mechanism of Sanmiao Pill on Gouty Arthritis Based on Network Pharmacology


Authors: Qian, Huiqin; Jin, Qianqian; Liu, Yichen; Wang, Ning; Chu, Yuru; Liu, Bingbing; Liu, Yan; Jiang, Wanli; Song, Yong

Sanmiao pill (SMP), a Chinese traditional formula, had been used to treat gouty arthritis (GA). However, the active compounds and underlying mechanism remained unclear. Hence, network pharmacology and molecular docking were utilized to explore bioactive compounds and potential mechanism of action of SMP in treating GA. In the study, the compounds of SMP, corresponding targets, and GA-related targets were mined from various pharmacological databases. Then, herb-compound-target, compound-target, PPI, and target-pathway networks were constructed. Ultimately, molecular docking was carried out to verify the predicted results. The results indicated that 47 active compounds, 338 targets, and 144 disease targets were collected. Network analysis implied thatPhellodendron chinenseSchneid. played a vital role in the whole formula. Moreover, 7 compounds (quercetin, kaempferol, wogonin, rutaecarpine, baicalein, beta-sitosterol, and stigmasterol) and 4 targets (NFKB1, RELA, MAPK1, and TNF) might be the kernel compounds and targets of SMP against GA. According to GOBP and KEGG pathway enrichment analysis and target-pathway network, SMP might exert a therapeutic role in GA by regulating numerous biological processes and pathways, including lipopolysaccharide-mediated signaling pathway, positive regulation of transcription, Toll-like receptor signaling pathway, JAK-STAT signaling pathway, NOD-like receptor signaling pathway, and MAPK signaling pathway. The results of molecular docking showcased that 11 pairs of compound with targets had tight binding strength. Thereinto, 4 compounds of MAPK1 and 5 compounds of NFKB1 possessed a better combination, suggesting that MAPK1 and NFKB1 might be considered as therapeutic targets in treatment of GA. This study verified that SMP had synergistic effect on GA by multicomponents, multitargets, and multipathways.

Aptamer-based optical manipulation of protein subcellular localization in cells


Authors: Xie, Sitao; Du, Yulin; Zhang, Yu; Wang, Zhimin; Zhang, Dailiang; He, Lei; Qiu, Liping; Jiang, Jianhui; Tan, Weihong

Protein-dominant cellular processes cannot be fully decoded without precise manipulation of their activity and localization in living cells. Advances in optogenetics have allowed spatio-temporal control over cellular proteins with molecular specificity; however, these methods require recombinant expression of fusion proteins, possibly leading to conflicting results. Instead of modifying proteins of interest, in this work, we focus on design of a tunable recognition unit and develop an aptamer-based near-infrared (NIR) light-responsive nano-platform for manipulating the subcellular localization of specific proteins in their native states. Our results demonstrate that this nanoplatform allows photocontrol over the cytoplasmicnuclear shuttling behavior of the target RelA protein (a member of the NF-kappa beta family), enabling regulation of RelA-related signaling pathways. With a modular design, this aptamer-based nanoplatform can be readily extended for the manipulation of different proteins (e.g., lyso-zyme and p53), holding great potential to develop a variety of label-free protein photoregulation strategies for studying complex biological events.

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