Analytical Data
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Gene name
CLDN7
- Application
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Alternative Names
CLDN7；CEPTRL2；CPETRL2；Claudin-7
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95471
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Expression Region
1-211aa
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AA Sequence
MANSGLQLLGFSMALLGWVGLVACTAIPQWQMSSYAGDNIITAQAMYKGLWMDCVTQSTG MMSCKMYDSVLALSAALQATRALMVVSLVLGFLAMFVATMGMKCTRCGGDDKVKKARIAM GGGIIFIVAGLAALVACSWYGHQIVTDFYNPLIPTNIKYEFGPAIFIGWAGSALVILGGA LLSCSCPGNESKAGYRVPRSYPKSNSSKEYV
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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
CLDN7 (Claudin-7) is a pivotal member of the claudin family of tight junction proteins, playing a crucial role in the regulation of paracellular permeability and maintaining epithelial barrier integrity. Recent studies have indicated that aberrant expression of CLDN7 is associated with various pathological conditions, including cancer progression, where it may contribute to enhanced invasiveness and metastasis. Researchers are increasingly interested in the functional characterization of CLDN7 as a therapeutic target, and its potential implications in diseases characterized by disrupted epithelial barriers. Additionally, given the importance of tight junctions in embryonic development and tissue homeostasis, understanding CLDN7's role may provide insights into developmental biology and tissue engineering. Recombination techniques have enabled the production of CLDN7 recombinant proteins for further investigation, allowing for detailed studies on its structural properties, interaction with other cellular components, and the nuances of its involvement in cell signaling pathways. Overall, the study of CLDN7 not only enhances our understanding of tight junction mechanics but also opens new avenues for developing interventions for diseases linked to tight junction dysfunction.
