Analytical Data
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Gene name
VEGFR-3/FLT4
- Application
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Alternative Names
FLT41; FLT4; PCL; Fms-Related Tyrosine Kinase 4; Tyrosine-protein kinase receptor FLT4
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 85% as determined by SDS-PAGE.
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Uniprot
P35916
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Expression Region
Tyr25~Ile776
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Protein Length
Partial
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Molecular Weight
88kDa
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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 3 (VEGFR-3), also known as Flt-4, is a receptor tyrosine kinase primarily involved in lymphangiogenesis and the regulation of lymphatic endothelial cell biology. The significance of VEGFR-3 in angiogenesis, lymphangiogenesis, and immune response has prompted extensive research into its role in various physiological and pathological contexts, particularly in cancer progression and metastasis. Dysregulation of VEGFR-3 signaling is associated with numerous diseases, including tumors that exploit lymphatic pathways for metastasis, underlining the receptor's potential as a therapeutic target. The generation of recombinant VEGFR-3 proteins has enabled detailed studies of its structure-function relationships and interactions with ligands, such as VEGF-C and VEGF-D, which are crucial for understanding its signaling mechanisms. These studies contribute to the development of novel therapeutic strategies aimed at modulating VEGFR-3 activity, offering promising avenues for cancer therapy and lymphatic disease treatment. As such, the investigation of VEGFR-3 recombinant proteins represents a vital area of focus in vascular biology and therapeutic development.
