| WB | 1/1000-1/2000 | Human,Mouse,Rat |
| IF | 1/20-1/50 | Human,Mouse,Rat |
| IHC | 1/100-1/200 | 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 | CVID9; Kinase PKC delta; KPCD; MAY1; nPKC delta; PCKd; PKC delta; PKCD; PKCdelta; PRKC delta; Prkcd; Protein Kinase C delta; Protein kinase C delta VIII; Protein Kinase Cdelta; Tyrosine protein kinase PRKCD;;p-PKC delta (Y313) |
| WB Predicted band size | Calculated MW: 78 kDa ; Observed MW: 77 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 |
| Immunogen | A synthesized peptide derived from human PKC delta around the phosphorylation site of Y313 |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.05% BSA and 50% glycerol. |
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以下是关于Phospho-PKCδ (Y311)抗体的3篇参考文献的简要概括(注：文献为虚拟示例，实际研究中请核实具体来源)：
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1. **文献名称**：*Tyrosine 311 phosphorylation of PKCδ regulates oxidative stress-induced apoptosis in neuronal cells*
**作者**：Li, X. et al.
**摘要**：研究报道PKCδ在氧化应激下通过Y311位点的磷酸化被激活，该磷酸化事件由c-Abl激酶介导，促进线粒体途径凋亡，揭示了其在神经退行性疾病中的潜在作用。
2. **文献名称**：*Phosphorylation of PKCδ at Tyr311 modulates its kinase activity in breast cancer progression*
**作者**：Wang, Y. et al.
**摘要**：本文证明HER2信号通过Src激酶磷酸化PKCδ的Y311位点，增强其激酶活性，进而促进乳腺癌细胞侵袭和转移，提示该位点作为治疗靶点的潜力。
3. **文献名称**：*PKCδ tyrosine phosphorylation at residue 311 is essential for DNA damage-induced apoptosis in leukemia cells*
**作者**：Kim, S. et al.
**摘要**：研究发现，化疗药物诱导的DNA损伤通过Y311磷酸化激活PKCδ，导致其转位至线粒体并触发caspase依赖性凋亡，为白血病耐药性机制提供了新见解。
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**注意**：以上文献为示例，实际研究中建议通过PubMed、Web of Science或抗体供应商(如CST、Abcam)提供的参考文献列表获取真实文献。搜索时可使用关键词：**PKCδ Y311 phosphorylation**、**PKCdelta Tyr311 antibody** 或结合相关通路(如凋亡、癌症)进行筛选。
**Background of Phospho-PKCδ (Y311) Antibody**
The Phospho-PKCδ (Y311) antibody is designed to detect protein kinase C delta (PKCδ) when phosphorylated at tyrosine residue 311. PKCδ, a member of the novel PKC subfamily, is a serine/threonine kinase involved in diverse cellular processes, including apoptosis, proliferation, differentiation, and stress responses. Its activity is tightly regulated by post-translational modifications, such as phosphorylation. Phosphorylation at Y311. located in the catalytic domain, is critical for modulating PKCδ’s enzymatic activity, substrate specificity, and subcellular localization.
This phosphorylation event is often linked to oxidative stress, DNA damage, or activation of tyrosine kinase receptors (e.g., EGFR, Src). Studies suggest that Y311 phosphorylation enhances PKCδ’s pro-apoptotic functions, particularly in contexts like cancer, neurodegeneration, and cardiovascular diseases. For instance, in response to genotoxic stress, phosphorylated PKCδ (Y311) translocates to the nucleus, promoting cell cycle arrest or apoptosis by interacting with substrates such as p73 or DNA repair proteins.
The Phospho-PKCδ (Y311) antibody is widely used in research to investigate PKCδ activation dynamics in signaling pathways and disease models. Specificity for the phosphorylated Y311 epitope enables precise detection in techniques like Western blotting, immunofluorescence, or immunohistochemistry. Understanding PKCδ regulation via Y311 phosphorylation provides insights into therapeutic targeting of PKCδ-associated pathologies, including chemoresistance in cancers or ischemic injury.
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