Analytical Data
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Gene name
CDH20
- Application
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Alternative Names
CDH7L3
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HBT6
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Expression Region
Trp61~Phe274
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Molecular Weight
31kDa
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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
CDH20, or Cadherin-20, is a member of the cadherin superfamily, which plays a crucial role in cell adhesion, tissue morphogenesis, and cellular signaling. It is particularly important in neural and epithelial tissues, influencing cell interactions and the structural integrity of tissues. Research on CDH20 has gained attention due to its potential implications in various physiological and pathological processes, including development, cancer progression, and neurodegenerative diseases. Understanding the function and mechanisms of CDH20 can provide insights into its role in cellular organization and communication. Additionally, the production and characterization of recombinant CDH20 protein offers a valuable tool for studying its biological properties in vitro. Such studies can help elucidate the structure-function relationships of cadherins and identify how alterations in CDH20 expression or function may contribute to disease. By using techniques such as protein expression in cell lines and functional assays, researchers aim to dissect the signaling pathways influenced by CDH20 and explore its potential as a therapeutic target. This recombinant protein research not only advances our understanding of cadherin biology but also opens avenues for the development of novel strategies in regenerative medicine and cancer therapy, making CDH20 a protein of significant interest in the field of cellular and molecular biology.
