Analytical Data
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基因名
VEGFR1
- Application
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别名
VEGFR1；FLT；FRT；VEGFR1；Vascular endothelial growth factor receptor 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P17948
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表达区间
25-688aa
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氨基酸序列
SGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERL SITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAI YIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPL DTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHR QTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNK RASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNT SVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGL PATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIV NVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHN HSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVV ADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLK LSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIM NVSLQDSGTYACRARNVYTGEEILQKKEITIRGEHCNKKAVFSRISKFKS TRNDCTTQSNVKH
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Vascular Endothelial Growth Factor Receptor 1 (VEGFR1) is a key player in the regulation of angiogenesis, the process through which new blood vessels form from pre-existing ones. It is primarily involved in mediating the effects of vascular endothelial growth factors (VEGFs), which are crucial for embryonic development, wound healing, and pathological processes such as cancer progression. VEGFR1 is known to have a high affinity for VEGF, but its precise role in signaling pathways remains complex, as it can both promote and inhibit downstream effects depending on the context and availability of ligands. Research has increasingly focused on recombinant VEGFR1 proteins to elucidate its biochemical properties, interactions with ligands, and the mechanisms through which it influences endothelial cell behavior. These studies aim to provide insights into the therapeutic potential of targeting VEGFR1 in diseases characterized by abnormal angiogenesis, such as cancer and diabetic retinopathy. By investigating the structure and function of recombinant VEGFR1, scientists hope to develop novel strategies for inhibiting tumor growth and metastasis, offering new avenues for effective treatment options. This research is vital for understanding the dual role of VEGFR1 and its potential as a biomarker or therapeutic target in various angiogenesis-related disorders.
