Analytical Data
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Gene name
Claudin-4/CLDN4 Protein-VLP
- Application
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Alternative Names
CPE-R; CPER; CPETR; CPETR1; WBSCR8; hCPE-R; Clostridium Perfringens Enterotoxin Receptor 1; Williams-Beuren Syndrome Chromosomal Region 8 Protein
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Species
Human
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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
O14493
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Expression Region
Met1~Arg81
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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
Claudin-4 (CLDN4) is a critical tight junction protein that plays a significant role in maintaining epithelial barrier integrity and regulating paracellular permeability. It is highly expressed in various tissues, including the gastrointestinal tract and pancreatic cells, and has been implicated in several diseases, including cancer. In particular, CLDN4 is of interest due to its upregulation in pancreatic ductal adenocarcinoma, making it a potential target for therapeutic intervention and diagnostic applications. The use of Virus-Like Particle (VLP) technology to produce recombinant proteins has gained attention for its ability to mimic natural viruses while being non-infectious. VLPs can present multiple copies of a target protein on their surface, enhancing immune responses and facilitating the study of protein interactions and functions. Research on CLDN4/CLDN4 Protein-VLP aims to leverage this technology for developing efficient vaccines or immunotherapeutics against cancers with CLDN4 overexpression. Additionally, VLPs offer a valuable platform for investigating the structure and function of CLDN4 in a controlled environment, aiding in the understanding of its role in cellular processes and pathogenesis. The combination of CLDN4 research with VLP technology holds promise for both therapeutic and diagnostic advancements, potentially leading to improved management strategies for diseases associated with altered CLDN4 expression.
