Analytical Data
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Gene name
VEGFR1
- Application
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Alternative Names
Flt1; Fms-Related Tyrosine Kinase 1; Vascular Permeability Factor Receptor; Fms-like tyrosine kinase 1; Tyrosine-protein kinase receptor FLT
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Species
Human
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Source
HEK293
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17948
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Expression Region
Ser27~lle328
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Molecular Weight
50kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
Protein Description
Vascular Endothelial Growth Factor Receptor 1 (VEGFR1) is a significant receptor in the VEGF signaling pathway, primarily involved in angiogenesis, the process of new blood vessel formation. Angiogenesis is crucial in various physiological and pathological contexts, including wound healing, tissue repair, and tumor growth. The dysregulation of this process is associated with numerous diseases, notably cancer, where tumors often exploit angiogenic pathways to sustain their growth and metastasis. Research into VEGFR1 has garnered interest due to its complex role as both a signaling receptor and a decoy receptor that can inhibit the actions of other VEGF isoforms. Understanding the structure, function, and interactions of VEGFR1 is essential for developing targeted therapies that modulate angiogenesis, offering potential treatments for cancer and other diseases where VEGF signaling is disrupted. Recombinant VEGFR1 proteins have been instrumental in these studies, enabling detailed investigations into receptor functionality and facilitating high-throughput screening of potential drug candidates. Furthermore, VEGFR1's role in immune responses indicates its broader implications beyond angiogenesis, making it a crucial target for research aimed at improving therapeutic strategies in oncology and regenerative medicine.
