Analytical Data
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Gene name
Claudin-4/CLDN4 Protein-VLP
- Application
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Alternative Names
CLDN4; claudin 4; CPETR, CPETR1; claudin-4; Clostridium perfringens enterotoxin receptor 1; CPE R; hCPE R; WBSCR8; Williams Beuren syndrome chromosomal region 8 protein;
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Species
Human
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O14493
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Expression Region
M1-V209
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Protein Length
Full Length
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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 tight junction protein primarily found in epithelial tissues, playing a crucial role in maintaining cell polarity and regulating paracellular permeability. Its dysregulation is associated with various pathological conditions, including cancer, where it is overexpressed in several tumors, making it a potential target for cancer immunotherapy. Researchers have increasingly focused on developing recombinant proteins and virus-like particles (VLPs) that encapsulate CLDN4 to enhance immune responses, aiming to create effective vaccines or therapeutic agents. The presentation of CLDN4 on VLPs can mimic the natural structure and function of the protein, facilitating the induction of robust humoral and cellular immune responses. This approach not only provides a platform for therapeutic immunization but also holds promise for targeted delivery strategies in clinical applications. By employing CLDN4/VLP systems, scientists aim to establish innovative treatment modalities for cancers that exhibit CLDN4 overexpression. Understanding the interaction between the immune system and CLDN4 presented on VLPs could yield critical insights into designing effective immunotherapeutics or vaccines targeting various malignancies.
