| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | 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 |
| Aliases | NOS, INOS, NOS2A, HEP-NOS |
| Entrez GeneID | 4843; |
| WB Predicted band size | 130kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Rat |
| Immunogen | Peptide sequence around phosphorylation site of Tyrosine 151 (Q-Y-Y(p)-G-S) derived from Human iNOS. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide and 30% glycerol. |
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以下是关于iNOS (Phospho-Tyr151)抗体的相关文献示例(注：文献信息为模拟示例，实际引用需根据真实研究调整)：
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1. **文献名称**: *"Tyrosine Phosphorylation of iNOS at Tyr151 Regulates Enzymatic Activity in Macrophages"*
**作者**: Smith A, et al.
**摘要**: 该研究首次报道iNOS在Tyr151位点的磷酸化可通过增强四氢生物蝶呤(BH4)结合来稳定其二聚体结构，从而提升一氧化氮合成活性。研究使用Phospho-Tyr151特异性抗体验证了LPS/IFN-γ刺激下巨噬细胞中该位点的磷酸化动态。
2. **文献名称**: *"Role of iNOS Phosphorylation in Sepsis-Induced Systemic Inflammation"*
**作者**: Chen L, et al.
**摘要**: 通过Phospho-Tyr151抗体检测，发现脓毒症小鼠模型中iNOS Tyr151磷酸化水平显著升高，且与NF-κB信号激活相关。抑制该磷酸化可减轻炎症损伤，提示其作为潜在治疗靶点。
3. **文献名称**: *"Development and Validation of a Phosphospecific Antibody for iNOS Tyr151"*
**作者**: Johnson R, et al.
**摘要**: 研究团队开发了针对iNOS Tyr151磷酸化位点的多克隆抗体，并通过肽竞争实验和磷酸酶处理验证其特异性。该抗体成功应用于免疫印迹和免疫荧光，揭示了Tyr151磷酸化在细胞定位中的作用。
4. **文献名称**: *"iNOS Post-Translational Modifications in Atherosclerosis"*
**作者**: Wang Y, et al.
**摘要**: 利用Phospho-Tyr151抗体分析动脉粥样硬化斑块组织，发现iNOS的Tyr151磷酸化与氧化应激水平正相关，且促进斑块内炎症细胞浸润。机制研究表明，该修饰通过增强iNOS与SHP-2的相互作用调控下游信号。
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**注意**：以上文献为示例性质，具体研究需通过PubMed或Web of Science以关键词“iNOS Tyr151 phosphorylation”或抗体货号(如Cell Signaling Technology #XXXXX)检索真实文献。部分商业抗体官网(如CST、Abcam)也会提供相关参考文献。
The inducible nitric oxide synthase (iNOS), also known as NOS2. is an enzyme responsible for producing nitric oxide (NO) in response to inflammatory stimuli, such as cytokines or pathogens. Its activity is tightly regulated at transcriptional and post-translational levels, including phosphorylation. Phosphorylation at tyrosine residue 151 (Tyr151) has been identified as a key modification modulating iNOS function. This site-specific phosphorylation may influence enzyme stability, subcellular localization, or interactions with regulatory proteins, ultimately affecting NO output in conditions like sepsis, chronic inflammation, or cancer.
Antibodies targeting iNOS phosphorylated at Tyr151 (Phospho-Tyr151) are critical tools for studying the activation dynamics of iNOS in disease models. They enable researchers to detect and quantify the phosphorylated, active form of iNOS in techniques like Western blotting, immunohistochemistry, or immunofluorescence. Such antibodies help elucidate how tyrosine phosphorylation events regulate iNOS-driven NO signaling pathways, which play dual roles in host defense and tissue damage. Dysregulated iNOS activity is linked to pathologies including neurodegenerative diseases, cardiovascular disorders, and tumor progression. By specifically recognizing the phosphorylated Tyr151 epitope, these antibodies provide insights into post-translational mechanisms underlying iNOS-related therapeutic targets or biomarkers. Validation of specificity via knockout controls or phosphatase treatment is essential for accurate interpretation.
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