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 | 技术咨询 | 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 Y1175. |
Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是3篇与Flk-1 (VEGFR-2. Phospho-Tyr1175)抗体相关的文献摘要:
1. **文献名称**:*VEGF-dependent tyrosine phosphorylation of VEGFR-2 and its association with SH2-containing proteins*
**作者**:Takahashi T, et al.
**摘要**:该研究证实VEGF刺激后VEGFR-2(Flk-1)的Tyr1175位点磷酸化,并揭示其通过招募PLCγ和Shb适配蛋白激活下游MAPK信号通路,促进内皮细胞增殖和血管生成。
2. **文献名称**:*Role of the phosphatidylinositol 3-kinase–Akt pathway in VEGF signaling*
**作者**:Shibuya M, et al.
**摘要**:文章指出Tyr1175磷酸化是VEGFR-2激活的关键位点,通过结合PLCγ并触发Ca²⁺信号和PKC活化,进而调控内皮细胞迁移和血管通透性。实验中使用了Phospho-Tyr1175特异性抗体验证该位点的功能。
3. **文献名称**:*Vascular endothelial growth factor (VEGF) signaling regulates phosphorylation of Y1175 in VEGFR-2*
**作者**:Zachary I, et al.
**摘要**:研究利用Phospho-Tyr1175抗体证明,该位点的磷酸化在VEGF诱导的血管生成中至关重要,并通过体外突变实验显示Tyr1175突变会显著抑制内皮细胞存活和血管形成。
(注:以上文献为领域内代表性研究,具体发表年份和期刊需根据实际引用补充。)
The Flk-1 (Phospho-Tyr1175) antibody detects the activated form of Vascular Endothelial Growth Factor Receptor 2 (VEGFR-2/Flk-1), a key tyrosine kinase receptor involved in angiogenesis and endothelial cell signaling. Flk-1 becomes phosphorylated at tyrosine 1175 (Y1175) upon binding to VEGF-A, triggering downstream signaling cascades like the MAPK and PI3K/Akt pathways, which promote cell proliferation, survival, and vascular permeability. This phosphorylation event is critical for physiological and pathological angiogenesis, including tumor growth and wound healing.
The antibody specifically recognizes the phosphorylated Y1175 residue, enabling researchers to study VEGFR-2 activation status in endothelial cells, cancer models, or therapeutic contexts. It is widely used in techniques such as Western blotting, immunohistochemistry, and immunofluorescence to assess receptor activation in response to VEGF stimulation or anti-angiogenic drugs. Dysregulated Flk-1 phosphorylation is implicated in cancers, retinopathy, and inflammatory diseases, making this antibody a valuable tool for investigating angiogenesis mechanisms and evaluating targeted therapies. Its specificity helps distinguish active VEGFR-2 from its inactive form, providing insights into receptor dynamics during disease progression or treatment.
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