Analytical Data
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Gene name
Claudin-18/CLDN18.2 Protein-Nanodisc
- Application
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Alternative Names
CLDN18; CLDN18.2; Claudin-18.2; Claudin-18; DKFZp564B2062; SFTA5; SFTPJ
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Species
Human
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Source
Baculovirus
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Tag
C-Avi;N-His;C-Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56856-2
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Expression Region
M1-A200
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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-6 (CLDN6) is a member of the claudin family of proteins, which are integral components of tight junctions in epithelial tissues, playing crucial roles in maintaining cell-cell adhesion and regulating paracellular permeability. Dysregulation of CLDN6 expression has been associated with various cancers, making it an important target for therapeutic interventions. However, studying CLDN6 has been challenging due to its complex interactions within cellular membranes and its difficulty in purification and characterization. The use of nanodiscs—small, membrane-mimicking systems composed of phospholipids and scaffold proteins—provides a versatile platform for the reconstitution of membrane proteins in a stable, soluble form. Recent advancements in the design of CLDN6 protein-nanodisc complexes allow researchers to circumvent traditional obstacles in membrane protein research, facilitating detailed structural and functional studies. By employing recombinant DNA techniques to produce CLDN6 and integrate it into nanodiscs, researchers aim to elucidate the protein's biophysical properties, interactions with other membrane proteins, and its role in cellular contexts. Additionally, this approach holds promise for therapeutic applications, including the development of targeted drug delivery systems or vaccines that exploit the unique antigenic properties of CLDN6 in cancer immunotherapy. Overall, the combination of CLDN6 and nanodisc technology represents a cutting-edge strategy in membrane protein research, furthering our understanding of tight junction dynamics and their implications in health and disease.
