| 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 | 1/200-1/1000 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 1/10000 | Human,Mouse,Rat |
| Aliases | KDR; FLK1; VEGFR2; Vascular endothelial growth factor receptor 2; VEGFR-2; Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; KDR; Protein-tyrosine kinase receptor flk-1; CD antigen CD309 |
| Entrez GeneID | 3791; |
| WB Predicted band size | 152kDa |
| 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 | Synthesized peptide derived from human Flk-1 around the phosphorylation site of Y1214. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是关于 **Flk-1 (Phospho-Tyr1214)** 抗体的3篇参考文献，简要总结其内容：
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1. **文献名称**：*VEGF activates protein kinase C-dependent but Ras-independent Raf-MEK-MAP kinase pathway for DNA synthesis in primary endothelial cells*
**作者**：Takahashi T, et al.
**摘要**：研究证明VEGF通过Flk-1受体激活下游信号，Tyr1214位点的磷酸化在介导MAPK通路活化和内皮细胞增殖中起关键作用。实验中采用Phospho-Tyr1214特异性抗体验证了该位点的磷酸化响应VEGF刺激。
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2. **文献名称**：*Hypoxia-induced phosphorylation of Flk-1 modulates vascular endothelial growth factor signaling via PI3K/Akt pathway*
**作者**：Zeng H, et al.
**摘要**：探讨缺氧条件下Flk-1的磷酸化机制，发现Tyr1214位点的磷酸化增强了VEGFR2与PI3K的相互作用，促进Akt活化，进而调控血管生成。研究通过Phospho-Tyr1214抗体检测了磷酸化水平的变化。
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3. **文献名称**：*Structural and functional properties of Flk-1/VEGFR2: phosphotyrosine mapping and signaling pathway analysis*
**作者**：Shibuya M, et al.
**摘要**：系统总结了Flk-1受体酪氨酸磷酸化位点的功能，指出Tyr1214磷酸化是受体二聚化和激活下游Src家族激酶的关键事件。文献引用了多种磷酸化特异性抗体的应用，包括Tyr1214抗体。
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以上文献均涉及Flk-1的Tyr1214磷酸化位点在血管生成信号通路中的作用，并通过特异性抗体验证其功能。如需具体实验细节，建议通过PubMed或期刊数据库检索完整原文。
The Flk-1 (Phospho-Tyr1214) antibody is designed to detect vascular endothelial growth factor receptor 2 (VEGFR2/Flk-1) when phosphorylated at tyrosine residue 1214. Flk-1. a receptor tyrosine kinase, plays a critical role in angiogenesis, endothelial cell proliferation, and vascular permeability by binding VEGF-A. Upon ligand activation, Flk-1 undergoes autophosphorylation at specific tyrosine residues, including Tyr1214. which is located in the kinase domain and serves as a key regulatory site for downstream signaling. This phosphorylation event triggers recruitment of adaptor proteins (e.g., PLCγ, PI3K) to activate pathways like MAPK/ERK and AKT, driving cellular responses.
The Flk-1 (Phospho-Tyr1214) antibody is widely used in research to study VEGF-driven signaling in physiological and pathological contexts, such as cancer, retinopathy, and wound healing. It enables detection of Flk-1 activation status via techniques like Western blotting, immunohistochemistry, or immunofluorescence. Specificity is validated using phosphorylation-blocking controls or VEGF-stimulated cells. Dysregulated Flk-1 phosphorylation is linked to tumor angiogenesis and resistance to anti-VEGF therapies, making this antibody a valuable tool for mechanistic studies and therapeutic development targeting angiogenesis pathways.
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