Analytical Data
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Gene name
NMI
- Application
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Alternative Names
(Nmi)(N-myc and STAT interactor)
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Species
Human
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Source
E. coli
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Tag
N- His-GST & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13287
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Expression Region
62-202aa
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Molecular Weight
51.1 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
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Protein Description
NMI (N-myc Interactor) is a multifunctional protein that plays a critical role in various cellular processes, including transcriptional regulation, cell proliferation, and apoptosis. Initially discovered as an interactor of the N-myc oncogene, NMI has garnered significant interest due to its involvement in cancer biology, particularly in the context of neuroblastoma and other malignancies. Research indicates that NMI can modulate the activity of various transcription factors and signaling pathways, which positions it as a potential oncogenic or tumor-suppressive entity depending on the cellular context. Investigations into the structural properties of NMI have revealed the presence of specific functional domains that facilitate its interactions with other proteins and nucleic acids. Moreover, studies have suggested that dysregulation of NMI expression or function is implicated in tumorigenesis and cancer progression, making it a candidate for targeted therapies and a biomarker for various cancers. Ongoing research aims to elucidate the precise mechanisms by which NMI influences cancer cell behavior and to explore its potential as a therapeutic target, providing a deeper understanding of its role in cancer biology and enhancing the development of novel treatment strategies. Given its significant implications in cell signaling and cancer, the comprehensive study of NMI and its restructured variants could pave the way for innovative approaches in cancer therapy and precision medicine.
