Analytical Data
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Gene name
VEGFR-1
- 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
Pig
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
ACH73486.1
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Expression Region
Lys19~Leu146
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Molecular Weight
45kDa
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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
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Protein Description
Vascular Endothelial Growth Factor Receptor 1 (VEGFR-1) is a critical receptor involved in angiogenesis, the formation of new blood vessels from pre-existing ones, which plays a significant role in various physiological and pathological processes, including cancer progression, tissue repair, and embryonic development. The overexpression of VEGFR-1 has been associated with tumor growth and metastasis, making it a potential target for cancer therapy. Research on recombinant VEGFR-1 proteins has surged as scientists aim to better understand its structure, function, and mechanisms of action. These studies often involve the production of recombinant VEGFR-1 proteins in various expression systems, allowing for in-depth analysis of their biochemical properties, ligand-binding abilities, and downstream signaling pathways. By elucidating the interactions between VEGFR-1 and its ligands, researchers hope to identify novel therapeutic strategies, including monoclonal antibodies or small-molecule inhibitors that can disrupt VEGFR-1 signaling, potentially leading to improved clinical outcomes in cancer treatment and other diseases linked to aberrant angiogenesis. Moreover, recombinant VEGFR-1 proteins serve as valuable tools for screening and development of anti-angiogenic drugs, providing insights into their efficacy and safety profiles. Overall, the study of recombinant VEGFR-1 not only enhances our understanding of vascular biology but also opens avenues for innovative therapeutic approaches targeting angiogenesis-related disorders.
