Analytical Data
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Gene name
CLDN8
- Application
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56748
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Expression Region
Gln29~Arg81
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Molecular Weight
37kDa
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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
Claudin-8 (CLDN8) is a member of the claudin family of proteins, which play a critical role in the formation of tight junctions in epithelial and endothelial tissues. These tight junctions are essential for maintaining the selective permeability of cellular barriers, thus regulating the passage of ions and small molecules. Recent studies have highlighted the importance of CLDN8 in various physiological and pathological processes, including cancer progression and inflammation. Given its potential role as a biomarker and therapeutic target, the recombinant form of CLDN8 has garnered significant interest in the scientific community. Research has focused on the expression, purification, and characterization of CLDN8 to better understand its structural properties and functional mechanisms. Additionally, the generation of CLDN8 recombinant proteins facilitates the exploration of its interactions with other cellular components and signaling pathways. Understanding these interactions can provide insight into the role of CLDN8 in disease contexts and may lead to innovative strategies for targeted therapies. As such, investigating CLDN8 not only enhances our grasp of tight junction biology but also opens avenues for potential clinical applications in treating diseases associated with tight junction dysfunction.
