Analytical Data
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Gene name
CLDN15
- Application
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Alternative Names
CLDN15; Claudin-15
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56746
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Expression Region
1-128aa
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AA Sequence
MSMAVETFGFFMATVGLLMLGVTLPNSYWRVSTVHGNVITTNTIFENLWFSCATDSLGVYNCWEFPSMLALSGSTDSPASLSGGTGLLVRLMSIKGPCEGRRLASCRLSVRCKEAVCVQGIFRPAGHS
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Molecular Weight
39.82 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
Claudin 15 (CLDN15) is a member of the claudin family, which comprises tight junction proteins that play a critical role in maintaining epithelial barrier integrity and regulating paracellular transport. Recent studies have highlighted the involvement of CLDN15 in various physiological and pathological processes, including intestinal permeability, inflammatory diseases, and cancer metastasis. Its expression has been found to be altered in several cancers, suggesting potential roles in tumor biology and metastasis. Given its significant relevance, the research on CLDN15 recombinant proteins has gained attention. Producing these proteins in a recombinant system allows for detailed functional studies, including their role in tight junction assembly and the impact of mutations on their function. Furthermore, recombinant CLDN15 can be utilized in therapeutic strategies, aiming to restore barrier integrity in diseases associated with dysregulated tight junctions. Understanding the structure-function relationship of CLDN15 through recombinant protein studies could provide insights into its mechanism of action and how it can be targeted for drug development. Overall, the research on CLDN15 recombinant proteins is essential for uncovering its biological functions and therapeutic potentials in various diseases.
