Analytical Data
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Gene name
CLDN2
- Application
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Alternative Names
SP82
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Species
Mouse
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O88552
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Expression Region
Asn29~Gln81
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Molecular Weight
25kDa
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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
CLDN2, or Claudin-2, is a member of the claudin family of tight junction proteins, which play a crucial role in maintaining the integrity of epithelial and endothelial barriers. These proteins regulate paracellular permeability and are essential for various physiological processes, including ion transport and tissue homeostasis. Unlike other claudins, CLDN2 is known to form channels that allow selective permeability, particularly for cations. Its expression is upregulated in various pathological conditions, including inflammatory bowel disease (IBD) and certain cancers, indicating its involvement in disease progression and tissue remodeling. Researchers are increasingly focused on CLDN2 due to its dual role as a tight junction protein and a potential therapeutic target. Understanding its structure and function can provide insights into the mechanisms underlying barrier dysfunction in diseases characterized by increased permeability. Recent studies have utilized recombinant CLDN2 proteins to investigate their properties, such as channel conductance and interaction with other tight junction components. The characterization of CLDN2 at the molecular level will enhance our understanding of tight junction dynamics and facilitate the development of targeted therapies aimed at restoring barrier function in affected tissues. Overall, CLDN2's significance in both normal physiology and disease pathogenesis makes it a vital subject of research in the field of cell biology and medicine.
