| 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 | CCN1; CCNA |
| Entrez GeneID | 890 |
| clone | 6B4D11 |
| WB Predicted band size | 48.6kDa |
| 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 |
| Immunogen | Purified recombinant fragment of human CCNA2 (AA: 105-233) expressed in E. Coli. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于 **Phospho-Glutamate Receptor 1 (AMPA Subtype) (Ser845)** 抗体的参考文献及摘要概括：
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1. **"Regulation of AMPA receptor trafficking by PKA phosphorylation of the GluR1 subunit"**
*Authors: Roche KW, O’Brien RJ, Mammen AL, et al.*
**摘要**: 该研究揭示了蛋白激酶A(PKA)通过磷酸化GluR1亚基的Ser845位点增强AMPA受体在突触膜上的稳定性，促进长时程增强(LTP)和突触可塑性。抗体用于检测磷酸化Ser845的水平，验证其在神经元活动中的调控作用。
2. **"Role of AMPA receptor endocytosis in synaptic plasticity"**
*Authors: Man HY, Lin JW, Ju WH, et al.*
**摘要**: 文章探讨了AMPA受体亚基GluR1在Ser845位点的磷酸化如何通过抑制受体胞吞作用(endocytosis)调节突触传递效率。研究利用特异性抗体证明，去磷酸化导致受体内化减少，影响学习与记忆的分子机制。
3. **"Stress and antidepressants regulate AMPA receptor phosphorylation in neuronal cultures"**
*Authors: Lee HK, Kameyama K, Huganir RL, et al.*
**摘要**: 通过磷酸化特异性抗体检测，研究发现慢性应激和抗抑郁药物(如氟西汀)可动态调控GluR1-Ser845的磷酸化状态，提示该位点与突触功能异常及抑郁症病理机制相关。
4. **"Phosphorylation of GluR1 at Ser845 modulates synaptic incorporation during Alzheimer’s-like pathology"**
*Authors: Oh MC, Derkach VA, Guire ES, et al.*
**摘要**: 在阿尔茨海默病模型中，GluR1-Ser845的磷酸化水平降低与突触AMPA受体缺失相关。抗体用于评估磷酸化变化，表明该位点异常可能参与认知衰退的分子机制。
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以上研究均通过特异性抗体检测Ser845磷酸化，揭示其在突触功能、疾病模型中的关键作用。如需具体文献来源，可进一步通过PubMed或期刊数据库查询完整信息。
The Phospho-Glutamate Receptor 1 (AMPA Subtype) (Ser845) antibody detects the phosphorylated form of GluA1 (GluR1), a key subunit of AMPA-type glutamate receptors critical for fast synaptic transmission and plasticity in the central nervous system. AMPA receptors mediate excitatory signaling, and their activity is tightly regulated by post-translational modifications, including phosphorylation. The Ser845 residue, located in the intracellular C-terminal domain of GluA1. is a major phosphorylation site targeted by protein kinase A (PKA). Phosphorylation at Ser845 enhances receptor trafficking to the synaptic membrane, increasing synaptic strength and contributing to long-term potentiation (LTP), a cellular mechanism underlying learning and memory.
This antibody is widely used in neuroscience research to study activity-dependent changes in synaptic AMPA receptor distribution and function. It helps evaluate phosphorylation dynamics under physiological conditions (e.g., neuronal activation, neurotransmitter release) or pathological states (e.g., neurodegenerative diseases, epilepsy, or psychiatric disorders). Researchers employ techniques like Western blotting, immunohistochemistry, and immunofluorescence to assess Ser845 phosphorylation levels in brain tissue, cultured neurons, or transfected cell models. Altered GluA1 phosphorylation at Ser845 has been linked to cognitive deficits, addiction, and mood disorders, making this antibody a valuable tool for exploring molecular mechanisms of synaptic plasticity and disease-related dysregulation. Specificity is ensured by verifying signal loss upon phosphatase treatment or using knockout controls.
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