Analytical Data
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Gene name
VEGF165
- Application
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Alternative Names
VEGF165；VEGF；Vascular endothelial growth factor A. long form
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
27-191aa
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AA Sequence
APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPS CVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHN KCECRPKKDRARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQ LELNERTCRCDKPRR
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Molecular Weight
19 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 (VEGF)165 is a crucial isoform of the VEGF family, primarily known for its role in promoting angiogenesis, the formation of new blood vessels from pre-existing ones. This process is vital for normal physiological functions such as wound healing and menstrual cycle regulation, but it also plays a significant role in pathological conditions like cancer, diabetic retinopathy, and age-related macular degeneration. Due to its pivotal role in these processes, VEGF165 has garnered considerable attention in biomedical research. Scientists have focused on recombinant protein production of VEGF165 to better understand its biological functions and interactions within the vascular system. The recombinant VEGF165 protein is used extensively in in vitro and in vivo studies to elucidate the mechanisms of endothelial cell proliferation and migration. Furthermore, it has potential therapeutic applications; for instance, VEGF165 inhibitors are being explored in cancer therapies to restrict tumor growth by limiting its blood supply. Understanding the structure-function relationship of VEGF165 through recombinant techniques can facilitate the development of novel therapeutic agents, including anti-angiogenic drugs. Overall, VEGF165 recombinant protein research is a critical area of study contributing to advances in treating various diseases linked to abnormal blood vessel formation.
