Analytical Data
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Gene name
CECD
- Application
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Alternative Names
CECDCecropin-D
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Species
Bombyx mori
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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
O76146
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Expression Region
25-60aa
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Molecular Weight
7.8 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
The research background of CECD (C-Terminal Ectodomain of Cadherin) recombinant proteins revolves around their critical role in cell adhesion and signaling processes. Cadherins are a family of transmembrane proteins that mediate cell-cell adhesion in various tissues, playing pivotal roles in development, tissue maintenance, and homeostasis. The ectodomain of cadherins, particularly the C-terminal portion, is essential for the proper functioning of these proteins, influencing their adhesive properties and interactions with intracellular signaling pathways. With advancements in recombinant DNA technology, scientists have been able to produce CECD proteins in vitro, allowing for detailed studies of their structure-function relationships. Research efforts focus on understanding how CECD proteins contribute to cellular behaviors and how they might be exploited in therapeutic applications, such as in cancer treatment, where aberrant cadherin expression often correlates with metastatic potential. Additionally, CECD proteins are being investigated for their potential to serve as biomarkers or targets for drug development, as modulating cadherin-mediated interactions could offer new avenues for intervention in various diseases. This research is crucial for advancing our understanding of cellular mechanics and developing novel strategies for disease management.
