Analytical Data
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Gene name
VEGF121
- Application
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Alternative Names
VEGF121；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
P15692-9
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Expression Region
27-147aa
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AA Sequence
APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPS CVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHN KCECRPKKDRARQEKCDKPRR
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Molecular Weight
14 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 key regulator of angiogenesis, playing a crucial role in both physiological and pathological processes, including wound healing, tumor growth, and retinal neovascularization. Among the various isoforms of VEGF, VEGF121 is notable for its potent angiogenic properties, as it lacks the heparin-binding domain, leading to its increased solubility and diffusion in tissues. This characteristic makes VEGF121 particularly interesting for therapeutic applications, especially in conditions where enhanced blood vessel formation is desired. Research has focused on the recombinant production of VEGF121 to explore its biological functions, optimize delivery methods, and evaluate its potential in regenerative medicine and cancer therapy. Furthermore, studies have demonstrated that VEGF121 can promote endothelial cell proliferation, migration, and survival, making it a candidate for interventions in ischemic diseases. However, the challenge remains to balance the angiogenic effects with potential adverse outcomes, such as edema or abnormal vessel formation. Thus, ongoing research aims to elucidate the molecular mechanisms of VEGF121 action and its therapeutic efficacy, paving the way for innovative treatments that harness the power of angiogenesis while mitigating associated risks.
