Analytical Data
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Gene name
VEGF165
- Application
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Alternative Names
VEGF-AA; rHuVEGF165; VPF; Folliculostellate cell-derived growth factor; Glioma-derived endothelial cell mitogen
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Species
Human
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Source
P. pastoris
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15692-4
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Expression Region
A27-R191
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Protein Length
Partial
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Molecular Weight
20-26 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
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Protein Description
Vascular endothelial growth factor (VEGF) is a critical signaling protein that plays a significant role in angiogenesis, the formation of new blood vessels from pre-existing ones. Among its isoforms, VEGF165 is the most abundant and biologically active variant, which has been extensively studied for its involvement in various physiological and pathological processes, including embryonic development, wound healing, and tumor growth. The dysregulation of VEGF165 expression is linked to several diseases, particularly cancer, where it promotes tumor angiogenesis, facilitating tumor growth and metastasis. Consequently, VEGF165 has emerged as a potential therapeutic target, leading to the development of anti-angiogenic therapies aimed at inhibiting its function. Recombinant VEGF165 protein has been utilized in research to elucidate its mechanisms of action, assess its role in cellular signaling pathways, and evaluate its effects on endothelial cell proliferation and migration. The production of recombinant VEGF165 in various expression systems, including bacterial, yeast, and mammalian cells, has allowed for detailed studies of its biochemical properties and biological activities. Understanding the structure-function relationship of VEGF165 is crucial for designing specific inhibitors or modulators that can effectively interfere with its signaling in pathological conditions, thereby providing new strategies for treating diseases associated with abnormal angiogenesis. Overall, the study of recombinant VEGF165 protein not only enhances our understanding of vascular biology but also paves the way for novel therapeutic interventions in cancer and other angiogenesis-related diseases.
