Analytical Data
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Gene name
N-Cadherin
- Application
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Alternative Names
CDw325; CD325; CDHN; CDH2; Cadherin 2 Type 1; N-Cadherin
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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 95% as determined by SDS-PAGE.
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Uniprot
P19022
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Expression Region
Ser685~Asp784
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Molecular Weight
26kDa
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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
N-Cadherin, a member of the cadherin superfamily, plays a crucial role in cell adhesion, differentiation, and tissue morphogenesis, making it a significant focus of research in developmental biology and cancer studies. As an integral component of adherens junctions, N-Cadherin mediates cell-cell interactions and influences cellular signaling pathways. Alterations in its expression are often associated with various pathological conditions, including tumor progression and metastasis, where a switch from E-Cadherin to N-Cadherin is commonly observed in epithelial-mesenchymal transition (EMT). This transition enhances cellular motility and invasiveness, characteristics that are critical in cancer progression. The study of N-Cadherin recombinant proteins serves multiple purposes: it enables a deeper understanding of its structural and functional properties, facilitates investigations into its role in cell signaling and adhesion mechanisms, and aids in the development of potential therapeutic strategies targeting N-Cadherin-mediated pathways. Furthermore, recombinant N-Cadherin can be utilized in in vitro assays to elucidate its interactions with other proteins, advancing our knowledge of its implications in cellular processes. Given the importance of N-Cadherin in health and disease, ongoing research efforts aim to provide insights into its molecular mechanisms, which could pave the way for novel interventions in cancer therapy and regenerative medicine.
