Analytical Data
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Gene name
MYCN
- Application
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Alternative Names
Class E basic helix-loop-helix protein 37 ;bHLHe37
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Species
Human
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Source
Yeast
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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
P04198
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Expression Region
1-464aa
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Molecular Weight
51.6 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
MYCN is a member of the MYC family of oncogenes and is known to play a critical role in the development and progression of neuroblastoma, a common pediatric cancer. Amplification of the MYCN gene is associated with aggressive tumor behavior and poor prognosis in affected children. Research into MYCN has focused on understanding its biological functions, regulatory mechanisms, and interactions with other signaling pathways in oncogenesis. The production of recombinant MYCN proteins has become increasingly important for elucidating the molecular mechanisms underlying its activity and for identifying potential therapeutic targets. By using techniques such as recombinant DNA technology and protein expression systems, researchers can produce MYCN in a controlled laboratory setting, allowing detailed studies of its structure, function, and role in cell signaling. Such investigations have the potential to reveal novel inhibitors that could disrupt MYCN-driven tumor growth, ultimately leading to the development of more effective therapies for neuroblastoma and improving outcomes for patients with MYCN-amplified tumors. This area of research thus holds significant promise for advancing our understanding of cancer biology and for guiding the search for new treatment strategies.
