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
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P35917
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Expression Region
Pro30~Ile326
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Molecular Weight
37kDa
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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
VEGFR-3, also known as FLT4, is a receptor tyrosine kinase primarily involved in the regulation of lymphangiogenesis and blood vessel development. Its significance has increased in various fields of biomedical research, particularly in cancer biology, as it plays a crucial role in tumor metastasis and the formation of lymphatic vessels. The activation of VEGFR-3 by its ligands, mainly VEGF-C and VEGF-D, drives lymphatic endothelial cell proliferation and migration, which are critical processes in both normal physiological and pathological conditions. Understanding the molecular mechanisms regulating VEGFR-3 can provide insights into novel therapeutic strategies for cancer and lymphatic disorders. The production and characterization of recombinant VEGFR-3/FLT4 protein enable researchers to study its structure-function relationships and interactions with ligands and downstream signaling pathways. Furthermore, recombinant VEGFR-3 can be utilized in various assays to screen potential inhibitors, which could lead to the development of new treatments targeting lymphangiogenesis in diseases such as cancer, lymphedema, and inflammation. Thus, the study of VEGFR-3/FLT4 recombinant protein is essential for advancing our knowledge of lymphatic biology and developing innovative therapeutic approaches.
