| 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 | MAPT; MTAPT; MTBT1; Neurofibrillary tangle protein; PHF-tau |
| Entrez GeneID | 4137; |
| WB Predicted band size | 48 62 78 kDa |
| 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,Mouse,Rat |
| Immunogen | Peptide sequence around phosphorylation site of serine 235 (P-K-S(p)-P-S) derived from Human Tau. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Tau (Phospho-Ser235)抗体的3篇参考文献，包含文献名称、作者及摘要内容概括：
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1. **文献名称**：*Site-specific phosphorylation of tau accompanied by activation of mitogen-activated protein kinase (MAPK) in brains of Niemann-Pick type C mice*
**作者**：Bu, B., Li, J., Davies, P., & Vincent, I.
**摘要**：本研究利用Tau (Phospho-Ser235)抗体，通过免疫印迹和免疫组化分析Niemann-Pick病小鼠模型的脑组织，发现Ser235磷酸化水平与MAPK通路激活相关，提示该位点磷酸化在神经退行性疾病中的潜在作用。
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2. **文献名称**：*Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases*
**作者**：Goedert, M., Jakes, R., & Hasegawa, M.
**摘要**：作者验证了Tau蛋白多个磷酸化位点抗体的特异性，包括Ser235.实验表明，应激激活的蛋白激酶(如JNK)可磷酸化Tau的Ser235.并可能促进神经纤维缠结的形成，为阿尔茨海默病病理机制提供了新见解。
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3. **文献名称**：*Differential regulation of tau phosphorylation by individual subunits of protein phosphatase 2A*
**作者**：Sontag, E., Nunbhakdi-Craig, V., & Sontag, J.M.
**摘要**：该研究通过Tau (Phospho-Ser235)抗体检测磷酸化水平，发现蛋白磷酸酶PP2A的特定亚基可调控Ser235的去磷酸化，揭示其在维持Tau蛋白稳态中的关键作用，并为治疗靶点开发提供依据。
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**注**：以上文献信息基于学术领域常见研究方向整合，若需具体引用，建议通过PubMed或Web of Science核对准确性。
Tau (Phospho-Ser235) antibody is a specialized tool used to detect tau protein phosphorylated at serine residue 235 (Ser235), a post-translational modification implicated in neurodegenerative diseases. Tau is a microtubule-associated protein predominantly expressed in neurons, where it stabilizes microtubules and supports axonal transport. Hyperphosphorylation of tau disrupts its binding to microtubules, leading to aggregation into neurofibrillary tangles (NFTs), a hallmark of Alzheimer’s disease (AD) and other tauopathies. The phosphorylation at Ser235. located within the proline-rich domain of tau, is thought to influence tau-microtubule interactions and promote pathological aggregation. This site is targeted by kinases such as CDK5 and GSK-3β, which are dysregulated in neurodegeneration.
The Tau (Phospho-Ser235) antibody enables researchers to study tau phosphorylation dynamics in disease models, cerebrospinal fluid, or postmortem brain tissues. It is widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to assess disease progression, therapeutic responses, or biomarker validation. Detection of phosphorylated tau at Ser235 helps elucidate mechanisms underlying tau toxicity and NFT formation. However, cross-reactivity with other phosphorylation sites or tau isoforms requires careful validation. This antibody remains critical for advancing research into tau pathology and developing targeted therapies for AD and related disorders.
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