Analytical Data
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Gene name
N Cadherin Protein ---
- Application
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Species
Human
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NP_001783
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Expression Region
D160-A724
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Protein Length
Partial
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Molecular Weight
100-120 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
N-cadherin, a member of the cadherin family of proteins, plays a crucial role in cell adhesion, facilitating the interaction between adjacent cells in tissues. It is predominantly expressed in neural tissues and is involved in various biological processes, including neurite outgrowth, tissue morphogenesis, and the maintenance of tissue architecture. The study of recombinant N-cadherin protein has become increasingly important due to its implications in developmental biology and cancer research. Understanding the structural and functional properties of N-cadherin can reveal insights into the mechanisms of cell-cell adhesion and signaling pathways involved in cellular processes. Furthermore, its dysregulation has been associated with several pathological conditions, such as cancer metastasis and neurodevelopmental disorders. By utilizing recombinant DNA technology, researchers can produce N-cadherin in a controlled environment, enabling detailed studies of its function and interactions. This provides opportunities for therapeutic interventions that target cadherin-mediated pathways. The characterization of recombinant N-cadherin also aids in the development of biomaterials and tissue engineering applications, where promoting cell adhesion and communication is vital for tissue regeneration. Overall, the investigation into N-cadherin and its recombinant forms not only enhances our understanding of fundamental biological processes but also paves the way for advancing medical research and therapeutic strategies.
