Analytical Data
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Gene name
VEGF145
- Application
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Alternative Names
VEGF145;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
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Expression Region
1-395aa
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AA Sequence
MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEPAPGGGVEGVGARGVALKLFVQLLGCSRFGGAVVRAGEAEPSGAARSASSGREEPQPEEGEEEEEKEEERGPQWRLGARKPGSWTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGPPHSPSRRGSASRAGPGRASETMNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR
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Molecular Weight
43.5 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) plays a crucial role in angiogenesis, the process of forming new blood vessels, which is essential for normal development and healing, as well as for pathological conditions such as cancer. Among the various isoforms of VEGF, VEGF145, a variant that is generated through alternative splicing, has gained attention due to its unique properties and potential therapeutic applications. Research has shown that VEGF145 exhibits distinct biological activities compared to other isoforms, which may influence its role in vascular permeability and endothelial cell function. Understanding the specific functions of VEGF145 could provide insights into targeted therapies for diseases characterized by abnormal angiogenesis, such as tumors or diabetic retinopathy. The recombination of VEGF145 for experimental purposes enables the study of its effects in vitro and in vivo, offering a platform to explore its mechanisms and interactions with other cellular factors. This research is critical for developing innovative therapeutic strategies aimed at modulating angiogenesis, ultimately improving outcomes in various diseases linked to abnormal blood vessel growth.











