| 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 | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | AURA17; Dardarin antibody; ; Leucine rich repeat kinase 2; LRRK 2 antibody; LRRK2; LRRK2_HUMAN; PARK 8; PARK8; RIPK7; ROCO 2; ROCO2 |
| Entrez GeneID | 120892 |
| WB Predicted band size | Calculated MW: 286 kDa; Observed MW: 286 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 |
| Immunogen | A synthesized peptide derived from human Phospho-LRRK2 (S935) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于 **Phospho-LRRK2 (Ser395) 抗体** 的3篇参考文献，按文献名称、作者和摘要内容简要概括：
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1. **文献名称**: *"LRRK2 phosphorylation regulates its interaction with Rab GTPases"*
**作者**: Smith, J.P. et al.
**摘要**: 该研究通过Phospho-LRRK2 (Ser395)抗体验证了LRRK2在Ser395位点的磷酸化状态，并发现该修饰影响LRRK2与Rab蛋白(如Rab7L1)的相互作用，提示其在囊泡运输中的调控作用。抗体特异性通过磷酸酶处理和点突变实验验证。
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2. **文献名称**: *"Phosphorylation of LRRK2 at Ser395 modulates neuronal toxicity in Parkinson’s disease models"*
**作者**: Chen, L. et al.
**摘要**: 使用Phospho-LRRK2 (Ser395)抗体检测帕金森病细胞模型中LRRK2的磷酸化水平，发现Ser395磷酸化减少与α-突触核蛋白聚集和神经元死亡相关，表明该位点磷酸化可能具有神经保护作用。
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3. **文献名称**: *"Auto-phosphorylation of LRRK2 at Ser395 is regulated by cellular stress and kinase activity"*
**作者**: Wang, Y. et al.
**摘要**: 研究通过免疫印迹(使用Phospho-Ser395抗体)和质谱分析，证明LRRK2在氧化应激条件下Ser395位点的自磷酸化水平升高，且该过程依赖其激酶活性，提示其可能在细胞应激响应中发挥作用。
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**注**：以上文献为示例性质，实际文献需通过数据库(如PubMed、Google Scholar)以关键词 **"Phospho-LRRK2 Ser395"** 或 **"LRRK2 phosphorylation Ser395"** 检索。建议结合具体实验需求筛选近年研究。
Phospho-LRRK2 (Ser395) antibody is a specialized tool used to detect the phosphorylation of leucine-rich repeat kinase 2 (LRRK2) at serine residue 395. LRRK2. a large multidomain protein kinase, is implicated in regulating vesicular trafficking, autophagy, and inflammatory responses. Dysregulation of LRRK2. particularly through mutations like G2019S, is linked to familial and sporadic Parkinson’s disease (PD). Phosphorylation at Ser395. located in the non-catalytic COR domain, is a key post-translational modification influencing LRRK2’s kinase activity, interaction with binding partners, and subcellular localization. This site is phosphorylated by upstream kinases (e.g., PKA) or through autophosphorylation, modulating LRRK2’s role in signaling pathways.
The Phospho-LRRK2 (Ser395) antibody enables researchers to study LRRK2 activation states and regulatory mechanisms in disease models. It is widely used in Western blotting, immunofluorescence, and immunoprecipitation to assess phosphorylation levels in cell lines, brain tissues, or biofluids. Its specificity helps evaluate the efficacy of LRRK2 inhibitors in preclinical studies, as dephosphorylation at Ser395 often correlates with reduced kinase activity.
Research using this antibody has advanced understanding of LRRK2’s pathobiology, including its interaction with Rab GTPases and contribution to neuroinflammation or neuronal death in PD. Validated across species and sample types, it remains critical for exploring therapeutic strategies targeting LRRK2 hyperactivation.
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