Analytical Data
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Gene name
Cornulin
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简介
Cornulin protein is critical in cell dynamics, promoting proliferation and promoting G1/S cell cycle progression, inducing the key regulator CCND1. It actively participates in the NFKB1 and PI3K/AKT pathways and responds to pro-inflammatory cytokines. Cornulin Protein, Human (His) is the recombinant human-derived Cornulin protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UBG3
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Expression Region
M1-S140
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Protein Length
Partial
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Molecular Weight
17 kDa
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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
Cornulin is a member of the S100 protein family, known for its role in calcium-binding and involvement in various cellular processes, including differentiation, cell cycle progression, and inflammatory responses. Found predominantly in epithelial tissues, Cornulin's expression is notably upregulated in certain pathological conditions, such as inflammatory diseases and carcinogenesis, suggesting a potential role in cellular responses to stress and tissue repair. Research has indicated that Cornulin may participate in the regulation of skin hydration, barrier function, and defense against oxidative stress. Additionally, studies have suggested its involvement in signaling pathways that influence cell survival and apoptosis. Given its relevance in both normal physiological processes and disease states, recombinant Cornulin proteins have garnered attention for their potential therapeutic applications. Investigating the structural and functional aspects of Cornulin through recombinant protein production may provide insights into its mechanistic roles and offer new strategies for intervention in diseases associated with abnormal Cornulin expression. As such, the study of Cornulin and its recombinant forms is crucial for understanding its contributions to human health and disease, paving the way for innovative biomedical applications.
