Analytical Data
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Gene name
EDIL3
- Application
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Alternative Names
(Developmentally-regulated endothelial cell locus 1 protein)(Integrin-binding protein DEL1)
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Species
Human
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Source
Baculovirus
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43854
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Expression Region
24-480aa
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Molecular Weight
57.0 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
EDIL3, a member of the Epidermal Growth Factor (EGF) repeat-containing protein family, has emerged as a significant focus in cancer research due to its role in various cellular processes, including cell adhesion, migration, and proliferation. Originally identified as an important factor in the development and progression of several types of tumors, EDIL3 is known to interact with extracellular matrix components and regulate signaling pathways crucial for tumor microenvironment modulation. Studies have revealed that EDIL3 is often overexpressed in malignant tissues, contributing to the invasive and metastatic potential of cancer cells. Moreover, its expression levels have been correlated with poor clinical outcomes in patients, underscoring its potential as a prognostic marker. Researchers are increasingly interested in the functional mechanisms of EDIL3, as understanding its role may lead to novel therapeutic approaches targeting cancer metastasis. Additionally, the recombinant expression of EDIL3 protein enables the exploration of its biochemical properties and interactions, facilitating the development of inhibitors or antibodies that can disrupt its function. The ongoing investigation into EDIL3's structure-function relationship will further elucidate its contributions to tumor biology and potentially provide insights into new treatment modalities, making it a promising candidate for targeted cancer therapies.
