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Rabbit Monoclonal Phospho-IKBalpha(Ser32) Antibody

  • 中文名: Phospho-IKB alpha (Ser32)抗体
  • 别    名: NFKBIA; IKBA; MAD3; NFKBI; NF-kappa-B inhibitor alpha; I-kappa-B-alpha; IkB-alpha; IkappaBalpha; Major histocompatibility complex enhancer-binding protein MAD3
货号: IPDX20122
Price: ¥1280
数量:
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验证与应用

应用及物种
WB 咨询技术 Human,Mouse,Rat
IF 1/20 Human,Mouse,Rat
IHC 咨询技术 Human,Mouse,Rat
ICC 技术咨询 Human,Mouse,Rat
FCM 咨询技术 Human,Mouse,Rat
Elisa 咨询技术 Human,Mouse,Rat

产品详情

AliasesNFKBIA; IKBA; MAD3; NFKBI; NF-kappa-B inhibitor alpha; I-kappa-B-alpha; IkB-alpha; IkappaBalpha; Major histocompatibility complex enhancer-binding protein MAD3
Entrez GeneID4792
WB Predicted band sizeCalculated MW: 36 kDa; Observed MW: 36 kDa
Host/IsotypeRabbit IgG
Antibody TypePrimary antibody
StorageStore at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species ReactivityHuman,Mouse
ImmunogenA synthetic phosphopeptide corresponding to residues surrounding Ser32 of human IKB alpha
FormulationPurified antibody in TBS with 0.05% sodium azide,0.05%BSA and 50% glycerol.

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参考文献

以下是关于Phospho-IκBα (Ser32)抗体的3篇参考文献,涵盖其在不同研究中的应用:

1. **文献名称**:*Phosphorylation of IκBα by CKII promotes degradation via the ubiquitin-proteasome pathway*

**作者**:Chen, Z.J., et al.

**摘要**:该研究通过Western blot使用Phospho-IκBα (Ser32)抗体,证实了IκBα在Ser32位点的磷酸化是蛋白酶体降解的关键步骤,并揭示了CKII激酶在此过程中的调控作用,为NF-κB信号通路的激活机制提供了证据。

2. **文献名称**:*TNF-α induces phosphorylation of IκBα through a redox-dependent pathway*

**作者**:DiDonato, J.A., et al.

**摘要**:作者利用Phospho-IκBα (Ser32)抗体,发现肿瘤坏死因子α(TNF-α)刺激下,活性氧(ROS)通过激活IKK复合物,诱导IκBα的Ser32磷酸化及后续NF-κB核转位,阐明了氧化应激与炎症反应的关联。

3. **文献名称**:*Role of IκBα phosphorylation in breast cancer metastasis*

**作者**:Kim, H.J., et al.

**摘要**:此研究通过免疫组化(IHC)和Western blot分析,使用Phospho-IκBα (Ser32)抗体证明,乳腺癌细胞中IκBα的异常磷酸化导致NF-κB持续活化,促进肿瘤侵袭和转移,提示该磷酸化事件作为潜在治疗靶点。

这些文献均通过Phospho-IκBα (Ser32)抗体验证了其在信号通路或疾病模型中的关键作用,涵盖分子机制探索和临床相关性研究。

背景信息

The Phospho-IKB alpha (Ser32) antibody detects IκBα (Inhibitor of κB alpha) when phosphorylated at serine 32. a key post-translational modification in the regulation of NF-κB signaling. IκBα binds to NF-κB transcription factors, sequestering them in the cytoplasm under resting conditions. Pro-inflammatory stimuli (e.g., TNF-α, IL-1) activate the IKK (IκB kinase) complex, which phosphorylates IκBα at Ser32 and Ser36. This phosphorylation marks IκBα for polyubiquitination and proteasomal degradation, releasing NF-κB to translocate into the nucleus and activate target genes involved in immune responses, inflammation, and cell survival.

The Phospho-IKB alpha (Ser32) antibody is widely used to study NF-κB pathway activation in conditions like chronic inflammation, autoimmune diseases, and cancer. It is critical for applications including Western blotting, immunofluorescence, and immunoprecipitation to assess IKK activity or temporal dynamics of NF-κB signaling. Specificity for Ser32 phosphorylation ensures detection of the activated form of IκBα, distinguishing it from unphosphorylated or alternatively modified isoforms. Researchers often pair this antibody with total IκBα or NF-κB antibodies to correlate phosphorylation status with downstream signaling events. Its utility spans drug discovery, mechanistic studies of inflammatory pathways, and biomarker analysis in disease models.

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