Analytical Data
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Gene name
VE-Cadherin
- Application
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Alternative Names
CD144; 7B4; Cadherin 5 Type 2; VE-Cadherin; Cadherin,Vascular Endothelial
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P55284
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Expression Region
Asp251~Ile426
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Molecular Weight
25kDa
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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
VE-Cadherin, or vascular endothelial cadherin, is a critical adhesion molecule primarily expressed in endothelial cells that form the inner lining of blood vessels. It plays a pivotal role in maintaining vascular integrity, regulating cell-cell junctions, and influencing various biological processes such as angiogenesis and inflammation. Given its key function in maintaining endothelial barrier stability, VE-Cadherin has garnered significant attention in the context of various pathological conditions, including cancer metastasis, cardiovascular diseases, and inflammatory disorders. Research into recombinant VE-Cadherin proteins has advanced our understanding of its structural and functional properties, providing tools for studying cell adhesion dynamics and signaling pathways. The generation of recombinant VE-Cadherin allows for the elucidation of its role in endothelial cell behavior and interactions, facilitating the development of therapeutic strategies aimed at modulating vascular functionality. Furthermore, recombinant forms of VE-Cadherin can serve as potential biomarkers or therapeutic targets, given their involvement in disease progression. With ongoing advancements in protein engineering and molecular biology, the study of VE-Cadherin continues to unveil insights into the complexities of endothelial biology and its implications in health and disease.
