Analytical Data
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Gene name
NID
- Application
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Alternative Names
Entactin
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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
P14543
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Expression Region
Ala971~Cys1219
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Molecular Weight
32kDa
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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
NID (Nodal Interacting Domain) recombinants have garnered significant attention in the field of protein research due to their essential roles in various biological processes, including cell signaling, development, and disease progression. NID proteins, often involved in embryonic development and stem cell maintenance, have been identified as key regulators of mesodermal and endodermal cell fate decisions. Their interactions with other signaling pathways, particularly the TGF-beta superfamily, highlight their importance in maintaining cellular homeostasis and influencing differentiation. The study of NID recombinant proteins facilitates the understanding of complex cellular mechanisms and may lead to advancements in regenerative medicine and therapeutic interventions for disorders stemming from developmental anomalies. Researchers are employing various recombinant DNA technologies to produce and analyze these proteins, allowing for a deeper comprehension of their structure-function relationships, post-translational modifications, and interactions with other biomolecules. This research is critical for elucidating the underlying mechanisms of diseases such as cancer, where disruptions in signaling pathways linked to NID proteins often occur. Overall, understanding NID recombinants not only enhances our fundamental knowledge of developmental biology but also opens avenues for novel biomedical applications.
