| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | 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 | Calcium/calmodulin dependent protein kinase II; KCC2A |
| Entrez GeneID | 816/817/818 |
| clone | 4F7 |
| Host/Isotype | Mouse IgG1 |
| 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,Mouse,Rat |
| Immunogen | Synthetic peptide conjugated to KLH. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
+ +
以下是关于Phospho-CaMKII (Thr287)抗体的3篇参考文献及其摘要(部分可能涉及Thr286的同源位点，需结合亚型确认)：
1. **"CaMKII: A Biochemical Bridge Linking Learning and Memory"**
- **作者**: Lisman, J., et al.
- **摘要**: 该综述探讨了CaMKII在突触可塑性和记忆形成中的作用，重点分析了Thr286/287磷酸化如何解除自抑制结构域，使酶持续激活。文中引用了针对Thr287位点的特异性抗体在神经元活性检测中的应用。
2. **"Structural Insights into Autoregulation of CaMKIIβ via Phosphorylation at Thr287"**
- **作者**: Coultrap, S.J., Bayer, K.U.
- **摘要**: 通过晶体结构和生化实验，揭示CaMKIIβ亚型Thr287磷酸化后构象变化的机制，并利用Phospho-Thr287抗体验证其在体外激酶活性和神经元树突定位中的功能。
3. **"Targeted Mutation of CaMKII Autophosphorylation Sites Alters Long-Term Synaptic Plasticity"**
- **作者**: Elgersma, Y., et al.
- **摘要**: 研究通过基因突变小鼠模型发现，Thr287位点磷酸化缺陷导致CaMKIIβ的突触定位异常，影响LTP(长时程增强)。该研究使用Thr287磷酸化特异性抗体进行Western blot分析，证实突变体的磷酸化水平降低。
**注意**：Thr287常见于CaMKIIβ亚型(对应α亚型的Thr286)。若需Thr286相关文献或进一步验证抗体应用，建议补充检索。
Phospho-CaMKII (Thr287) antibodies are essential tools for studying the activation dynamics of calcium/calmodulin-dependent protein kinase II (CaMKII), a multifunctional serine/threonine kinase critical in neuronal signaling, synaptic plasticity, and memory formation. CaMKII is activated by calcium influx, which triggers its binding to calmodulin, leading to autophosphorylation at Thr287 (numbered as Thr286 in some rodent isoforms). This phosphorylation event sustains kinase activity even after calcium levels decline, a feature central to its role in long-term potentiation (LTP) and cellular memory.
The Thr287 autophosphorylation site resides within the regulatory domain of CaMKII. Phosphorylation at this residue disrupts the autoinhibitory interaction between the catalytic and regulatory domains, locking the kinase in a calcium-independent, constitutively active state. Antibodies targeting phospho-Thr287 specifically recognize this activated conformation, enabling researchers to track CaMKII activation in response to physiological stimuli (e.g., neuronal activity) or pathological conditions (e.g., ischemia, neurodegeneration).
These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate CaMKII-related signaling in brain tissue, cardiac cells, and disease models (e.g., Alzheimer’s, epilepsy, heart failure). Proper controls, including phosphorylation-blocking peptides or knockout validations, are critical to confirm specificity due to potential cross-reactivity with homologous phospho-epitopes. Understanding Thr287 phosphorylation dynamics provides insights into CaMKII’s dual roles as a synaptic modulator and a contributor to excitotoxicity in neurological disorders.
×
