Analytical Data
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Gene name
VEGFR-2
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简介
VEGFR-2 protein is an important tyrosine protein kinase receptor.As a cell surface receptor for VEGFA, VEGFC and VEGFD, it plays an important role in the regulation of angiogenesis, vascular development, permeability and embryonic hematopoiesis.It actively promotes endothelial cell proliferation, survival, migration, differentiation, and actin cytoskeletal reorganization.VEGFR-2 Protein, Mouse (HEK293, Fc) is the recombinant mouse-derived VEGFR-2 protein, expressed by HEK293 , with C-hFc labeled tag.
- Application
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Biological Activity
Measured by its ability to inhibit the VEGF-dependent proliferation of HUVEC human umbilical vein endothelial cells. The ED50 this effect is 4.894 ng/mL in the presence of 5 ng/mL recombinant human VEGF165, corresponding to a specific activity is 2.043×105 units/mg. Measured by its ability to inhibit the VEGF-dependent proliferation of HUVEC human umbilical vein endothelial cells.The ED50 for this effect is 4.894 ng/mL in the presence of 5 ng/mL recombinant human VEGF165, corresponding to a specific activity is 2.043×105 units/mg.
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Alternative Names
Vascular endothelial growth factor receptor 2; VEGFR-2; FLK-1; NYK; CD309
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Species
Mouse
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35918
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Expression Region
A20-E762
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AA Sequence
ASVGLPGDFLHPPKLSTQKDILTILANTTLQITCRGQRDLDWLWPNAQRDSEERVLVTECGGGDSIFCKTLTIPRVVGNDTGAYKCSYRDVDIASTVYVYVRDYRSPFIASVSDQHGIVYITENKNKTVVIPCRGSISNLNVSLCARYPEKRFVPDGNRISWDSEIGFTLPSYMISYAGMVFCEAKINDETYQSIMYIVVVVGYRIYDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPGTVAKMFLSTLTIESVTKSDQGEYTCVASSGRMIKRNRTFVRVHTKPFIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISMEKQSHMVSLVVNVPPQIGEKALISPMDSYQYGTMQTLTCTVYANPPLHHIQWYWQLEEACSYRPGQTSPYACKEWRHVEDFQGGNKIEVTKNQYALIEGKNKTVSTLVIQAANVSALYKCEAINKAGRGERVISFHVIRGPEITVQPAAQPTEQESVSLLCTADRNTFENLTWYKLGSQATSVHMGESLTPVCKNLDALWKLNGTMFSNSTNDILIVAFQNASLQDQGDYVCSAQDKKTKKRHCLVKQLIILERMAPMITGNLENQTTTIGETIEVTCPASGNPTPHITWFKDNETLVEDSGIVLRDGNRNLTIRRVRKEDGGLYTCQACNVLGCARAETLFIIEGAQEKTNLE
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Protein Length
Extracellular Domain
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Molecular Weight
138.21 kDa
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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 2 (VEGFR-2) is a critical receptor in angiogenesis, playing a pivotal role in the regulation of blood vessel growth and maintenance. It is primarily involved in mediating the effects of Vascular Endothelial Growth Factor (VEGF), which is essential for both physiological processes and pathological conditions, such as cancer and cardiovascular diseases. The study of VEGFR-2 recombinant protein has gained significant importance due to its potential therapeutic applications. Understanding the structure and function of VEGFR-2 can facilitate the development of targeted therapies aimed at inhibiting angiogenesis in tumor growth. Additionally, VEGFR-2 is a promising target for monoclonal antibodies and small molecule inhibitors that may improve treatment outcomes in various malignancies. Advances in recombinant protein technology have enabled the production of this protein in a more efficient manner, allowing for detailed studies of its signaling pathways and interactions with ligands. As research progresses, the characterization and functional analysis of VEGFR-2 recombinant proteins continue to provide insights into new treatment modalities, emphasizing the need for continued exploration of this receptor in both basic and translational research.
