Analytical Data
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Gene name
Claudin-1 Protein-VLP
- Application
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Alternative Names
CLD1; LILVASC; LSEMP1
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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
O95832 M1
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Expression Region
M1-V211
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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
Related Products
Protein Description
Claudin-1 is a crucial protein that forms tight junctions in epithelial and endothelial cells, playing a key role in maintaining the integrity of cellular barriers. Its dysregulation has been implicated in various pathological conditions, including cancer progression and inflammatory diseases. The development of Claudin-1 Protein Virus-Like Particles (VLPs) represents a novel approach for both therapeutic and diagnostic applications. By utilizing VLPs to present Claudin-1 in a native conformation, researchers aim to enhance the immune response against tumors that overexpress this protein. Moreover, this technology facilitates the study of Claudin-1's role in cellular processes and its potential as a biomarker for diseases. The ability to generate stable, non-infectious VLPs that mimic the structure of viruses, while displaying the Claudin-1 protein on their surface, provides an innovative platform for vaccine development and targeted drug delivery. Investigations into Claudin-1 VLPs are paving the way for improved strategies in immunotherapy, potentially leading to more effective treatments for cancers and other diseases associated with tight junction dysregulation.
