| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/100-1/300 | Human,Mouse,Rat |
| ICC | 1/100-1/500 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | p85, AGM7, p85-ALPHA, p55, p55-GAMMA, PIK3R1 |
| Entrez GeneID | 5295; |
| WB Predicted band size | 55,85kDa |
| 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 tyrosine 467 (L-Y(p)-E-E-Y) derived from Human PI3 Kinase p85/p55. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于 PI3 Kinase p85/p55 (phospho-Tyr467/199) 抗体的3篇参考文献，内容简洁概括：
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1. **"Regulation of PI3K signaling by tyrosine phosphorylation of the p85 subunit"**
*Author: Fruman, D.A. et al.*
**摘要**: 研究揭示了p85亚基的酪氨酸磷酸化(如Tyr467/199位点)在调节PI3K活性中的关键作用，通过抑制或增强其与催化亚基p110的相互作用，影响下游信号通路。
2. **"Phosphorylation of the p85 regulatory subunit of PI3K modulates its interaction with tyrosine-phosphorylated proteins"**
*Author: Cantley, L.C. et al.*
**摘要**: 该文献证实p85亚基的Tyr467/199磷酸化可改变其与受体酪氨酸激酶(如胰岛素受体)的结合能力，从而调控PI3K的膜定位及脂质激酶活性。
3. **"Tyrosine phosphorylation of p85 relieves its inhibitory activity in PI3K signaling"**
*Author: Vanhaesebroeck, B. et al.*
**摘要**: 实验表明，p85亚基在Tyr467/199位点的磷酸化会解除其对p110催化亚基的抑制作用，促进PI3K信号通路的激活，并增强细胞增殖和存活。
4. **"Role of PI3K p85 tyrosine phosphorylation in cancer progression"**
*Author: Engelman, J.A. et al.*
**摘要**: 研究探讨了p85亚基酪氨酸磷酸化(包括Tyr467/199)在肿瘤中的作用，发现其异常激活与癌症细胞的迁移、侵袭及耐药性密切相关。
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以上文献均聚焦于p85/p55亚基的酪氨酸磷酸化(Tyr467/199)对PI3K信号通路的调控机制及其生物学意义。建议结合具体实验需求选择引用。
The PI3 Kinase (phosphoinositide 3-kinase) p85/p55 regulatory subunits play a critical role in mediating downstream signaling of the PI3K-Akt pathway, which regulates cell growth, survival, and metabolism. Class IA PI3Ks consist of a catalytic subunit (p110) and a regulatory subunit (p85. p55. or p50). The p85 subunit (e.g., p85α, p85β) and its truncated splice variants (p55. p50) contain SH2 domains that bind phosphorylated tyrosine residues on activated receptor tyrosine kinases (RTKs) or adaptor proteins, thereby recruiting and activating the p110 catalytic subunit.
Phosphorylation at specific tyrosine residues, such as Tyr467 in p85α and Tyr199 in p55γ, is crucial for modulating PI3K activity. These phosphorylation events can either enhance or suppress interactions with signaling partners, depending on cellular context. For example, phosphorylation at Tyr467 (p85α) occurs in response to growth factor stimulation and may regulate autoinhibitory interactions between p85 and p110. promoting pathway activation. Similarly, Tyr199 phosphorylation in p55 influences its scaffolding function and downstream signaling.
The PI3 Kinase p85/p55 (phospho-Tyr467/199) antibody specifically detects these phosphorylation events, serving as a tool to study PI3K activation status in diseases like cancer, diabetes, and immune disorders. Dysregulation of PI3K signaling, often linked to tyrosine phosphorylation abnormalities, is a hallmark of tumorigenesis and metabolic syndromes. This antibody aids in elucidating mechanisms of PI3K-driven pathologies and evaluating therapeutic inhibitors targeting this pathway.
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