Analytical Data
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Gene name
VIL
- Application
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Alternative Names
Villin 1; VIL1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09327
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Expression Region
Met1~Lys320
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Molecular Weight
39.5kDa
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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
VIL (Vascular Inhibitory Protein) is a member of the class of proteins involved in various cellular processes, including angiogenesis and cell adhesion. Research on VIL recombinant proteins has gained prominence due to their potential therapeutic applications in cancer treatment and wound healing. These proteins can modulate the interaction between vascular endothelial cells and the extracellular matrix, thus influencing angiogenesis, which is critical in tumor growth and metastasis. The understanding of VIL’s structure and function at the molecular level allows for the engineering of recombinant versions that may have enhanced biological activities or reduced immunogenicity. Furthermore, VIL-related studies have suggested its role as a biomarker for various diseases, thereby opening avenues for diagnostic applications. The modulation of VIL pathways can provide insights into the development of new anti-angiogenic drugs, which could be pivotal in treating pathological conditions characterized by abnormal blood vessel formation. Additionally, the ability to produce VIL in recombinant systems ensures a consistent supply for research and potential therapeutic use, allowing scientists to explore its mechanistic roles further. Overall, the investigation of VIL recombinant proteins is essential for understanding their biological significance and developing novel therapeutic strategies that could leverage their unique properties in mitigating disease.
