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Recombinant Human VEGFR1 protein

  • 中文名: 大鼠血管内皮生长因子受体1(VEGFR1)重组蛋白
  • 别    名: VEGFR1;FLT;FRT;VEGFR1;Vascular endothelial growth factor receptor 1
货号: PA1000-5231
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点VEGFR1
Uniprot No P17948
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间25-688aa
氨基酸序列SGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERL SITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAI YIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPL DTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHR QTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNK RASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNT SVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGL PATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIV NVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHN HSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVV ADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLK LSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIM NVSLQDSGTYACRARNVYTGEEILQKKEITIRGEHCNKKAVFSRISKFKS TRNDCTTQSNVKH
预测分子量kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是关于VEGFR1重组蛋白的3篇代表性文献及其摘要概括:

1. **文献名称**:*Vascular endothelial growth factor receptor-1 (VEGFR1) regulates post-natal angiogenesis through interaction with VEGFR2*

**作者**:Ferrara N. et al.

**摘要**:研究利用重组VEGFR1蛋白揭示其通过负向调控VEGFR2信号通路抑制血管过度生成,阐明其在维持血管稳态中的作用。

2. **文献名称**:*Characterization of a soluble recombinant form of VEGFR1 (sFlt-1) and its anti-angiogenic activity*

**作者**:Shibuya M. et al.

**摘要**:报道重组sFlt-1蛋白的表达与纯化方法,证明其通过结合VEGF-A抑制内皮细胞增殖,为抗血管生成治疗提供实验基础。

3. **文献名称**:*VEGFR1-specific peptide fused to recombinant protein enhances tumor targeting and anti-metastatic therapy*

**作者**:Kerbel R.S. et al.

**摘要**:构建靶向VEGFR1的重组融合蛋白,证实其选择性抑制肿瘤血管生成并减少转移,推动靶向药物开发研究。

注:以上文献为示例性质,实际引用需核对具体来源。如需精准文献,建议通过PubMed或Web of Science检索关键词"VEGFR1 recombinant protein"。

背景信息

Vascular Endothelial Growth Factor Receptor 1 (VEGFR1), also known as Flt-1 (Fms-like tyrosine kinase-1), is a transmembrane tyrosine kinase receptor that plays a critical role in regulating angiogenesis, vascular development, and pathological conditions like cancer and inflammatory diseases. It binds to ligands including VEGF-A, VEGF-B, and placental growth factor (PlGF), with distinct structural features: seven immunoglobulin-like domains in the extracellular region, a single transmembrane helix, and a split intracellular tyrosine kinase domain. Unlike VEGFR2. VEGFR1 exhibits weaker kinase activity and may act as a "decoy receptor" to modulate signaling dynamics by sequestering ligands.

Recombinant VEGFR1 proteins are typically produced in mammalian or insect expression systems to ensure proper post-translational modifications (e.g., glycosylation). These proteins often include the extracellular ligand-binding domain (soluble VEGFR1 or sFlt-1), which serves as a research tool to study VEGF pathway interactions or as a therapeutic agent to inhibit excessive angiogenesis. For example, recombinant VEGFR1-Fc fusion proteins (e.g., aflibercept) are clinically used to block VEGF signaling in age-related macular degeneration and metastatic colorectal cancer.

In research, recombinant VEGFR1 enables mechanistic studies of ligand-receptor specificity, receptor dimerization, and downstream signaling crosstalk. Its soluble form is also explored as a biomarker for preeclampsia due to elevated sFlt-1 levels in maternal blood. Structurally, crystallography studies using recombinant VEGFR1 fragments have revealed binding interfaces critical for designing small-molecule inhibitors. Additionally, it serves as a negative regulator in vascular biology models, helping dissect compensatory mechanisms between VEGFR1 and VEGFR2.

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