Analytical Data
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Gene name
VEGFC
- Application
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Alternative Names
VEGFC；Vascular endothelial growth factor C
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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
P49767
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Expression Region
112-227aa
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AA Sequence
AHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFFKPPCVSVYR CGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRC MSKLDVYRQVHSIIRR
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Molecular Weight
46 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
VEGFC (Vascular Endothelial Growth Factor C) is a key protein in the VEGF family, primarily involved in lymphangiogenesis, the formation of lymphatic vessels, and angiogenesis, the formation of blood vessels. Its significance has been highlighted in numerous studies linking VEGFC to both normal physiological processes and various pathological conditions, including cancer, cardiovascular diseases, and lymphedema. In cancer, VEGFC has been implicated in promoting tumor metastasis by enhancing lymphatic vessel development, thereby facilitating the spread of cancer cells. Research on VEGFC recombinant proteins has gained momentum as it offers the potential to understand its biological functions in greater detail and develop therapeutic interventions. By producing VEGFC as a recombinant protein, researchers can investigate its structure, signaling pathways, and interactions with receptors such as VEGFR-3. Additionally, studying VEGFC in a controlled environment helps unravel its role in the vascular system and its implications in disease progression. The development of VEGFC-based therapies, encompassing either inhibition of its action to combat tumor growth or stimulation to promote wound healing and tissue regeneration, underscores the protein's dual potential as both a therapeutic target and a treatment agent. Thus, the study of recombinant VEGFC is an important facet of modern biomedical research, providing insights that could lead to novel strategies in treating diseases associated with vascular dysfunction.
