Analytical Data
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Gene name
VEGF-C
- Application
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Alternative Names
Flt4 ligand ;Flt4-LVascular endothelial growth factor-related protein ;VRP
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49767
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Expression Region
112-227aa
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Protein Length
Partial
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Molecular Weight
40.1 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 C (VEGF-C) is a pivotal protein involved in lymphangiogenesis, the process of forming new lymphatic vessels, and is a key regulator of endothelial cell function. Its role in promoting lymphatic endothelial cell proliferation and migration has made it a significant focus of research in both normal physiology and pathological conditions, such as cancer, inflammation, and lymphedema. In the context of tumor biology, VEGF-C is particularly notable for its capacity to facilitate metastasis by enhancing lymphatic spread of cancer cells, which underscores its potential as a therapeutic target. Recombinant VEGF-C protein studies have been instrumental in elucidating the molecular mechanisms underlying lymphangiogenesis and have paved the way for the development of novel therapeutic strategies aimed at modulating this process. Additionally, the exploration of VEGF-C’s interaction with its receptors, VEGFR-2 and VEGFR-3, and subsequent signaling pathways has highlighted its importance in vascular biology. Understanding the functional aspects of VEGF-C through recombinant protein studies not only contributes to a deeper comprehension of vascular development but also offers insights into innovative interventions for diseases characterized by aberrant lymphatic function. This has spurred interest in creating VEGF-C-based biomolecules or inhibitors that can regulate its activity, fostering a burgeoning field of research dedicated to targeting lymphangiogenesis therapeutically. As such, the study of recombinant VEGF-C continues to be a critical area of inquiry with wide-ranging implications in oncology, regenerative medicine, and beyond.
