Analytical Data
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Gene name
EG-VEGF
- Application
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Alternative Names
EG-VEGF；Prokineticin-1
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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
P58294
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Expression Region
20-105aa
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AA Sequence
AVITGACERDVQCGAGTCCAISLWLRGLRMCTPLGREGEECHPGSHKVPF FRKRKHHTCPCLPNLLCSRFPDGRYRCSMDLKNINF
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Molecular Weight
10 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
Endothelial growth factor B (EG-VEGF) is a recently identified member of the vascular endothelial growth factor family, specifically linked to the regulation of lymphangiogenesis and angiogenesis. As a crucial player in the development and maintenance of lymphatic endothelial cells, EG-VEGF has drawn considerable attention in the fields of immunology and oncology. Its expression is significantly upregulated in various pathological conditions, including tumors and inflammatory diseases, suggesting its role in promoting lymphatic vascular growth and remodeling. Research indicates that EG-VEGF might contribute to tumor metastasis through the facilitation of lymphatic invasion, making it a potential biomarker for tumor progression and a target for therapeutic interventions. The recombinant protein form of EG-VEGF has been studied for its functional characteristics in modulating lymphatic endothelial cell proliferation, migration, and survival. Understanding the molecular mechanisms and signaling pathways involved in EG-VEGF activity could lead to novel strategies for treating diseases characterized by abnormal lymphatic function, such as cancer and lymphedema. Overall, the study of EG-VEGF recombinant protein offers promising avenues for both basic research and clinical applications in vascular biology.
