Phospho-RELA (S281) Antibody
Description
Introduction to Phospho-RELA (S281) Antibody
This antibody targets the phosphorylated RELA protein, a key component of the NF-κB complex, which regulates genes involved in cellular proliferation, apoptosis, and stress responses. Phosphorylation at Ser281 modulates RELA’s transcriptional activity and nuclear translocation, making this antibody essential for investigating post-translational regulation of NF-κB .
Target Biology: RELA/p65 and Phosphorylation at Ser281
RELA (p65) forms heterodimers with other NF-κB subunits (e.g., p50) to regulate gene expression. Phosphorylation at Ser281 is implicated in fine-tuning NF-κB activity, though its functional role is less characterized compared to other sites like Ser536 or Ser276. Detection of this modification helps elucidate context-specific signaling mechanisms, such as cytokine-induced activation or stress responses .
Applications in Research
The Phospho-RELA (S281) Antibody has been validated for:
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Western blotting: Detects phosphorylated RELA in lysates from stimulated cells.
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Immunohistochemistry (IHC): Localizes phospho-RELA in tissue sections.
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Immunofluorescence (IF): Visualizes subcellular distribution (e.g., nuclear vs. cytoplasmic).
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Flow cytometry (FCM): Quantifies phospho-RELA expression in cell populations .
Research Findings and Validation Data
While specific studies using this antibody are not publicly detailed in the provided sources, its design and validation data suggest utility in:
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Pathway activation studies: Monitoring NF-κB activation in response to TNF-α or other stimuli.
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Disease models: Investigating phosphorylated RELA in cancer, autoimmune diseases, or chronic inflammation.
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Kinase/phosphatase assays: Identifying upstream regulators of Ser281 phosphorylation .
Technical Considerations
Product Specs
Target Background
- These findings suggest that resveratrol induces chondrosarcoma cell apoptosis through a SIRT1-activated NF-κB (p65 subunit of NF-κB complex) deacetylation mechanism, demonstrating its anti-chondrosarcoma activity in vivo. PMID: 28600541
- Enhanced IL-1β production by the v65Stop mutant is partially attributed to the induction of DNA binding and the transcriptional activity of NF-κB. PMID: 30332797
- A study utilizing integrative analysis of transcriptomic, metabolomic, and clinical data proposes a model for GOT2 transcriptional regulation. This model emphasizes the cooperative phosphorylation of STAT3 and the direct joint binding of STAT3 and p65/NF-κB to the proximal GOT2 promoter as critical elements. PMID: 29666362
- These results delineate a novel role for MKRN2 in negatively regulating NF-κB-mediated inflammatory responses, working cooperatively with PDLIM2. PMID: 28378844
- Compared to patients with NF-κB-94 ins/del ATTG ins/ins and ins/del genotypes, multiple myeloma patients with the del/del genotype exhibited the highest myeloma cell ratio. PMID: 30211233
- The riboflavin transporter-3 (SLC52A3) 5'-flanking regions contain NF-κB p65/Rel-B-binding sites, which are crucial for mediating SLC52A3 transcriptional activity in esophageal squamous cell carcinoma (ESCC) cells. PMID: 29428966
- Akirin-2 might serve as a novel biomarker for imatinib resistance. Targeting Akirin-2, NFκB, and β-catenin genes could potentially provide a strategy to overcome imatinib resistance in CML. PMID: 29945498
- The NF-κB-94ins/del ATTG genotype might serve as a novel biomarker and potential target for immune thrombocytopenia. PMID: 30140708
- Our findings suggest that melatonin exerts anti-tumor activities against thyroid carcinoma by inhibiting p65 phosphorylation and inducing reactive oxygen species. Radio-sensitization by melatonin may offer clinical benefits in thyroid cancer. PMID: 29525603
- Lutein's antiproliferative effect is mediated by the activation of the NrF2/ARE pathway and the blocking of the NF-κB signaling pathway. Lutein treatment reduced NF-κB signaling pathway-related NF-κB p65 protein expression. PMID: 29336610
- Furthermore, the present study suggests that SNHG15 might be involved in the nuclear factorkappaB signaling pathway, inducing the epithelial-mesenchymal transition process and promoting renal cell carcinoma invasion and migration. PMID: 29750422
- This revealed that the overexpression of p65 partially reversed SOX4 downregulation-induced apoptosis. In conclusion, our findings demonstrated that inhibition of SOX4 significantly induced melanoma cell apoptosis through the downregulation of the NF-κB signaling pathway. This suggests a novel approach for treating melanoma. PMID: 29767266
- Downregulation of HAGLROS may alleviate lipopolysaccharide-induced inflammatory injury in WI-38 cells through modulation of the miR-100/NF-κB axis. PMID: 29673591
- Our observations suggest that the RelA activation domain and multiple cofactor proteins work cooperatively to prime the RelA-DNA binding domain and stabilize the RelA:DNA complex in cells. PMID: 29708732
- Results show that MKL1 influences the chromatin structure of pro-inflammatory genes. Specifically, MKL1 defines histone H3K4 trimethylation landscape for NF-κB-dependent transcription. PMID: 28298643
- The study examined the association of SIRT2 and the p53/NF-kB p65 signaling pathways in preventing high glucose-induced vascular endothelial cell injury. Results demonstrated that SIRT2 overexpression is associated with deacetylation of p53 and NF-kB p65, which inhibits high glucose-induced apoptosis and vascular endothelial cell inflammation response. PMID: 29189925
- In conclusion, the spindle cell morphology is likely induced by RelA activation (p-RelA S468) through IKKε upregulation in human herpesvirus 8 vFLIP-expressing EA hy926 cells. PMID: 30029010
- High P65 expression is associated with doxorubicin-resistance in breast cancer. PMID: 29181822
- Reduced miR-138 expression enhanced the destruction of cartilage tissues among osteoarthritis patients, primarily through targeting p65. PMID: 28537665
- The present results indicate that vascular smooth proliferation is regulated by the activation of the NF-κB p65/miR17/RB pathway. As NF-κB p65 signaling is activated in and is a master regulator of the inflammatory response, these findings may provide a mechanism for the excessive proliferation of VSMCs under inflammation during vascular disorders. This may identify novel targets for the treatment of vascular... PMID: 29115381
- Real-time PCR and western blotting revealed that Huaier extract decreased p65 and c-Met expression and increased IκBα expression, while paclitaxel increased p65 expression and reduced IκBα and c-Met expression. The molecular mechanisms may involve the inhibition of the NF-κB pathway and c-Met expression. PMID: 29039556
- Ghrelin effectively suppressed TNF-α-induced inflammatory factors' (including ICAM-1, VCAM-1, MCP-1, and IL-1β) expression by inhibiting AMPK phosphorylation and p65 expression, both in HUVEC and THP-1. PMID: 28653238
- These data indicate that the MALAT1/miR146a/NF-κB pathway plays a key role in LPS-induced acute kidney injury (AKI), providing novel insights into the mechanisms of this therapeutic candidate for the treatment of the disease. PMID: 29115409
- Cytosolic AGR2 contributed to cell metastasis, attributed to its stabilizing effect on the p65 protein, which subsequently activated NF-κB and facilitated epithelial-to-mesenchymal transition (EMT). PMID: 29410027
- We provide evidence that S100A7 also inhibits YAP expression and activity through p65/NFκB-mediated repression of ΔNp63, and S100A7 represses drug-induced apoptosis by inhibiting YAP. PMID: 28923839
- This study shows the age-related reductions in serum IL-12 in healthy non-obese subjects. PMID: 28762199
- NF-κB p65 potentiated tumor growth by suppressing a novel target, LPTS. PMID: 29017500
- p65 siRNA retroviruses could suppress the activation of the NFκB signaling pathway. PMID: 28990087
- miR-215 facilitated HCV replication through inactivation of the NF-κB pathway by inhibiting TRIM22, presenting a novel potential target for HCV infection. PMID: 29749134
- Acute inflammation after injury initiates crucial regenerative signals, partly through NF-κB-mediated signaling that activates neural stem cells to reconstitute the olfactory epithelium. The loss of RelA in the regenerating neuroepithelium disrupts the homeostasis between proliferation and apoptosis. PMID: 28696292
- PAK5-mediated phosphorylation and nuclear translocation of NF-κB-p65 promotes breast cancer cell proliferation in vitro and in vivo. PMID: 29041983
- While 3-methyladenine rescues cell damage. Our data suggest that I/R promotes NF-κB p65 activity mediated by Beclin 1-mediated autophagic flux, thereby exacerbating myocardial injury. PMID: 27857190
- Taken together, these data indicate that upregulation of ANXA4 leads to activation of the NF-κB pathway and its target genes in a feedback regulatory mechanism through the p65 subunit, resulting in tumor growth in GBC. PMID: 27491820
- p65 is significantly upregulated in BBN-induced high invasive BCs and human BC cell lines. Our studies have also uncovered a new PTEN/FBW7/RhoGDIα axis, which is responsible for the oncogenic role of RelA p65 in promoting human BC cell migration. PMID: 28772241
- p65 O-GlcNAcylation promotes lung metastasis of cervical cancer cells by activating CXCR4 expression. PMID: 28681591
- We demonstrated that pristimerin suppressed tumor necrosis factor α (TNFα)-induced IκBα phosphorylation, translocation of p65, and expression of NFκB-dependent genes. Moreover, pristimerin decreased cell viability and clonogenic ability of Uveal melanoma (UM) cells. A synergistic effect was observed in the treatment of pristimerin combined with vinblastine, a frontline therapeutic agent, in UM. PMID: 28766683
- This study establishes p65 as a novel target of IMP3 in increasing glioma cell migration and underscores the significance of the IMP3-p65 feedback loop for therapeutic targeting in GBM. PMID: 28465487
- High NF-κB p65 expression is associated with resistance to doxorubicin in breast cancer. PMID: 27878697
- In colon cancer cell migration, activin utilizes NFkB to induce MDM2 activity, leading to the degradation of p21 in a PI3K-dependent mechanism. PMID: 28418896
- The study examined melatonin's role in cell senescence, autophagy, sirtuin 1 expression, and acetylation of RelA in hydrogen peroxide-treated SH-SY5Y cells. PMID: 28295567
- The data demonstrate that miR-125b regulates nasopharyngeal carcinoma cell proliferation and apoptosis by targeting the A20/NF-κB signaling pathway. miR-125b acts as an oncogene, whereas A20 functions as a tumor suppressor. PMID: 28569771
- NF-κB physically interacts with FOXM1 and promotes transcription of the FOXM1 gene. NF-κB directly binds to the FOXM1 gene promoter. Silencing p65 attenuates FOXM1 and β-catenin expression. NF-κB activation is required for the nuclear translocation of FOXM1 and β-catenin. FOXM1 and β-catenin positively regulate NF-κB. Knockdown of β-catenin and FOXM1 downregulates p65 protein and NF-κB-dependent reporter... PMID: 27492973
- PTX treatment of THP-1 macrophages for 1 hour induced marked intranuclear translocation of NF-κB p65. Low-dose PTX inhibited the M2 phenotype and induced the M1 phenotype through TLR4 signaling, suggesting that low-dose PTX can alter the macrophage phenotype, whereas clinical doses can kill cancer cells. These results suggest that the anticancer effects of PTX are due to both its cytotoxic and immunomodulatory activities. PMID: 28440494
- Sphk1 induced NF-κB-p65 activation, increased expression of cyclin D1, shortened the cell division cycle, and thus promoted proliferation of breast epithelial cells. PMID: 27811358
- Expression of NF-κB/p65 holds prognostic value in high-risk non-germinal center B-cell-like subtype diffuse large B-cell lymphoma. PMID: 28039454
- The NFKB1 -94 insertion/deletion ATTG polymorphism is associated with decreased risks for lung cancer, nasopharyngeal carcinoma, prostate cancer, ovarian cancer, and oral squamous cell carcinoma. PMID: 28039461
- PU.1 supports TRAIL-induced cell death by inhibiting RelA-mediated cell survival and inducing DR5 expression. PMID: 28362429
- EGF and TNFα cooperatively promoted the motility of HCC cells mainly through NF-κB/p65 mediated synergistic induction of FN in vitro. These findings highlight the crosstalk between EGF and TNFα in promoting HCC, and provide potential targets for HCC prevention and treatment. PMID: 28844984
- The Brd4 acetyllysine-binding protein of RelA is involved in the activation of polyomavirus JC. PMID: 27007123
- MUC1-C activates the NF-κB p65 pathway, promotes occupancy of the MUC1-C/NF-κB complex on the DNMT1 promoter, and drives DNMT1 transcription. PMID: 27259275
Q&A
What is RELA/NF-κB p65 and why is phosphorylation at S281 significant?
RELA (also known as NF-κB p65) is a subunit of the NF-κB transcription factor complex that regulates genes controlling inflammation, immune cell development, cell cycle, proliferation, and cell death . The NF-κB complex typically consists of a heterodimer of a Rel family member (RelA, c-Rel, or RelB) and either NF-κB1 or NF-κB2 subunits, with RelA and NF-κB1 being the most common pair .
Phosphorylation at S281 is part of the complex regulatory mechanism that controls RELA activity. While the specific consequence of S281 phosphorylation is not as extensively characterized as other sites, it appears to play a role in regulating RELA's function in a manner distinct from other phosphorylation sites. Research suggests it may modulate RELA's interaction with other proteins or its DNA binding specificity, similar to how phosphorylation at other serine residues affects RELA function .
How does phosphorylation at different serine residues affect RELA function?
RELA undergoes phosphorylation at multiple serine residues, each with distinct functional consequences:
Phosphorylation at S276 or S536 has been shown to enhance the assembly of phospho-RelA with the histone acetyltransferase p300, which increases acetylation at lysine 310 and ultimately enhances transcriptional activity . This demonstrates how phosphorylation can work in concert with other post-translational modifications to fine-tune RELA function.
What are the primary applications for Phospho-RELA (S281) antibodies?
Based on the search results, Phospho-RELA (S281) antibodies are employed in several key techniques:
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Western blotting: For detection of phosphorylated RELA in cell or tissue lysates
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Immunohistochemistry (IHC): For visualization of phosphorylated RELA in tissue sections
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Flow cytometry: For cellular analysis of phosphorylation status
The recommended dilutions for optimal results vary by application, typically 1:100-1:300 for IHC and 1:5000 for ELISA . These antibodies enable researchers to track the dynamic phosphorylation status of RELA in response to various stimuli, providing insights into NF-κB regulation under different physiological and pathological conditions.
How can researchers validate the specificity of phospho-RELA (S281) antibodies?
Validating antibody specificity is critical for obtaining reliable results. For phospho-RELA (S281) antibodies, consider implementing the following validation strategies:
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Phosphatase treatment control: Treat samples with lambda phosphatase to remove phosphorylation and confirm loss of antibody signal .
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Peptide competition assay: Pre-incubate the antibody with the phosphorylated peptide immunogen to block specific binding .
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Phospho-mutant controls: Compare antibody reactivity between wild-type cells and those expressing S281A mutant RELA, which cannot be phosphorylated at this position .
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Multiple technique validation: Confirm phosphorylation status using complementary techniques (e.g., Western blot, mass spectrometry) .
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Stimulus-response validation: Verify expected changes in phosphorylation following treatment with known NF-κB activators like TNFα or PMA/Ionomycin .
For instance, one study evaluating phospho-antibodies found that "the rabbit monoclonal antibody D1R1R uniquely and robustly detected endogenous phosphorylated alpha-synuclein at Ser129 in rat primary culture of ENS without any non-specific bands" . Similar rigorous testing should be applied to phospho-RELA (S281) antibodies.
What are the optimal experimental conditions for detecting RELA S281 phosphorylation?
To optimize detection of S281 phosphorylation, researchers should consider:
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Fixation and preservation: Immediate fixation is crucial as phosphorylation is often transient. For flow cytometry studies, one protocol recommends "immediately fixed using 20:1 ratio (9.5 mLs) of 4% FA diluted in 1× PBS for 10 minutes at room temperature to preserve phosphorylation status" .
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Stimulation timing: NF-κB activation is highly dynamic. In one study, "TNFα induced both P-p65 and total p65 translocation significantly relative to time zero (untreated cells), with P-p65 peaking at 20 minutes, preceding a total p65 peak at 25 minutes" . Therefore, time course experiments are recommended.
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Lysis conditions: Use phosphatase inhibitors (e.g., sodium fluoride, sodium orthovanadate) in lysis buffers to prevent dephosphorylation during sample preparation .
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Sample handling: Minimize freeze-thaw cycles as recommended for antibody storage: "For short term storage and frequent use, store at 4°C for up to one month. Avoid repeated freeze-thaw cycles" .
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Control selection: Include both positive controls (cells stimulated with TNFα) and negative controls (unstimulated cells or phosphatase-treated samples) .
How does RELA S281 phosphorylation relate to other post-translational modifications?
RELA undergoes multiple post-translational modifications that work in concert to regulate its activity. The interplay between these modifications creates a complex regulatory network:
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Phosphorylation and acetylation crosstalk: Phosphorylation at S536 has been shown to stimulate acetylation on K310, enhancing transcriptional activity . It's possible that S281 phosphorylation similarly affects acetylation patterns.
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Phosphorylation and ubiquitination: Some phosphorylation events can trigger ubiquitination and subsequent degradation. For RELA, "ubiquitinated by RNF182, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response" .
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Phosphorylation and methylation interactions: "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" .
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Site-specific effects: Different phosphorylation sites have distinct effects. For instance, "The phosphorylation of serine 328 by Chk1 is triggered by DNA damage and regulates the interaction of p50 with specific NF-κB binding elements based on the κB-site nucleotide sequence" . Similar site-specific effects may exist for S281 phosphorylation.
Research to determine how S281 phosphorylation fits into this modification network would provide valuable insights into NF-κB regulation.
What experimental approaches can elucidate the functional significance of RELA S281 phosphorylation?
To investigate the functional consequences of S281 phosphorylation, researchers could employ:
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Site-directed mutagenesis: Generate S281A (phospho-deficient) and S281D/E (phospho-mimetic) mutants to study the impact on RELA function . For example, "Reconstitution of RelA-deficient murine embryonic fibroblasts with RelA S276A or RelA S536A decreased TNF-α-induced acetylation of lysine 310 and expression of the endogenous NF-κB-responsive E-selectin gene" .
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Kinase identification: Use kinase inhibitors or knockdown/knockout approaches to identify the kinase(s) responsible for S281 phosphorylation, similar to how "phosphorylation of p105 at S903 and S907 by GSK3β" was identified .
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DNA binding assays: Determine whether S281 phosphorylation affects DNA binding specificity using techniques like chromatin immunoprecipitation (ChIP) or electrophoretic mobility shift assays (EMSA) .
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Proteomic approaches: Use mass spectrometry-based methods to identify proteins that differentially interact with phosphorylated versus non-phosphorylated S281 RELA .
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Imaging flow cytometry: Apply techniques like those described in search result , which "demonstrate the application of IFC to simultaneously assess phosphorylation of p65 and its cellular localization" .
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Gene expression profiling: Compare transcriptional responses in cells expressing wild-type versus S281 mutant RELA to identify genes specifically regulated by this phosphorylation site.
How might S281 phosphorylation contribute to gene-specific transcriptional regulation?
Phosphorylation of NF-κB subunits can lead to gene-specific effects on transcription. For instance, "NF-κB phosphorylation controls transcription in a gene-specific manner, offering new opportunities to selectively target NF-κB for therapeutic benefit" . Several mechanisms could explain how S281 phosphorylation might contribute to such specificity:
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Sequence-specific DNA binding: Similar to how "S328 phosphorylation reduces the affinity of p50 for κB-sites with a cytosine, but not an adenine, at the -1 position" , S281 phosphorylation might affect RELA's affinity for specific DNA sequences.
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Cofactor recruitment: Phosphorylation status can determine which cofactors interact with RELA. For example, "Interacts with HDAC1; the interaction requires non-phosphorylated RELA. Interacts with CBP; the interaction requires phosphorylated RELA" .
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Chromatin modification patterns: Phosphorylated RELA might recruit different chromatin-modifying enzymes to specific promoters, as suggested by the finding that "Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities" .
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Integration with other signaling pathways: S281 phosphorylation might respond to specific cellular stimuli or stress conditions, allowing for context-dependent gene regulation.
Understanding these mechanisms would advance our knowledge of how NF-κB achieves specificity in its transcriptional responses despite regulating hundreds of genes.
What factors influence the reproducibility of phospho-RELA (S281) detection?
Several factors can affect the reproducibility of phospho-RELA detection experiments:
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Antibody quality: Different lots or sources may vary in specificity and sensitivity. "The D1R1R antibody uniquely and robustly detected endogenous phosphorylated protein...without any non-specific bands" , demonstrating the importance of antibody selection.
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Phosphatase activity: Rapid dephosphorylation during sample preparation can lead to inconsistent results. "Following incubation, samples were immediately fixed...to preserve phosphorylation status" .
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Stimulation protocols: The timing, concentration, and type of stimulus affect phosphorylation patterns. "TNFα induced both P-p65 and total p65 translocation significantly relative to time zero (untreated cells), with P-p65 peaking at 20 minutes" .
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Fixation methods: Improper fixation can result in epitope masking or loss of phosphorylation signal. One study noted detection challenges "even when the transferred membrane is fixed with an optimized protocol" .
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Cell culture conditions: Cell density, passage number, and serum conditions can influence baseline phosphorylation levels and responsiveness to stimuli.
Standardizing these variables is essential for obtaining consistent and reliable results.
What are the optimal normalization strategies for quantifying S281 phosphorylation?
Proper normalization is critical for accurate quantification of phosphorylation:
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Total protein normalization: Compare phospho-RELA signal to total RELA levels to account for variations in total protein expression. "Cell-Based ELISA Kits...contain antibodies to measure both the phosphorylated and the total protein" .
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Housekeeping protein controls: Use stable reference proteins like GAPDH or β-actin as loading controls for Western blot analyses.
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Ratio-based quantification: "These two proteins are simultaneously detected in the same microplate well, allowing signals derived from the target protein to be normalized to that of the second protein. This permits corrections for well-to-well variation" .
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Internal cellular controls: In flow cytometry or imaging studies, use unstimulated cells within the same sample as internal references.
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Standard curve calibration: For quantitative ELISAs, generate standard curves using recombinant phosphorylated proteins when available.
These approaches help control for technical variations and enable meaningful comparisons across experimental conditions.
What are the emerging techniques for studying RELA phosphorylation dynamics?
Recent technological advances offer new possibilities for investigating RELA phosphorylation:
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Live-cell imaging with phospho-specific sensors: Genetically encoded biosensors that change conformation or FRET efficiency upon phosphorylation could enable real-time visualization of RELA S281 phosphorylation dynamics.
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Single-cell phosphoproteomics: Emerging techniques allow measurement of phosphorylation events at the single-cell level, revealing heterogeneity within cell populations.
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Imaging flow cytometry: As described in search result , this technique "demonstrate[s] the application of IFC to simultaneously assess phosphorylation of p65 and its cellular localization" .
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CRISPR-based screens: Genome-wide or targeted screens could identify novel regulators of S281 phosphorylation.
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Proximity labeling approaches: BioID or APEX2-based methods could identify proteins that interact specifically with phosphorylated RELA at S281.
These techniques promise to provide unprecedented insights into the spatial and temporal dynamics of RELA phosphorylation.
How might understanding S281 phosphorylation contribute to therapeutic strategies?
Insights into RELA S281 phosphorylation could inform novel therapeutic approaches:
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Targeted inhibition: If S281 phosphorylation regulates specific subsets of NF-κB target genes, inhibitors targeting this modification could provide more selective anti-inflammatory effects than global NF-κB inhibitors. This aligns with the observation that "NF-κB phosphorylation controls transcription in a gene-specific manner, offering new opportunities to selectively target NF-κB for therapeutic benefit" .
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Biomarker development: Phospho-S281 levels could serve as biomarkers for disease activity or treatment response in conditions involving dysregulated NF-κB signaling.
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Combination therapies: Understanding how S281 phosphorylation interacts with other regulatory mechanisms could suggest effective drug combinations that target multiple aspects of NF-κB regulation.
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Precision medicine approaches: If genetic variants affect S281 phosphorylation or its downstream effects, this could inform personalized treatment strategies for inflammatory or immune-mediated diseases.
The fundamental insights gained from studying S281 phosphorylation thus have potential translational implications that extend beyond basic research.
