Analytical Data
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Gene name
NLE1
- Application
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Alternative Names
AL022765; BC018399; FLJ10458; NLE 1; Nle; NLE1; NLE1_HUMAN; Notchless gene homolog; Notchless homolog 1 (Drosophila); Notchless homolog 1; Notchless protein homolog 1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NVX2
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Expression Region
2-485aa
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Molecular Weight
69.2 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
NLE1 (Numb-like E3 ubiquitin-protein ligase 1) is an important protein implicated in various biological processes, including cell proliferation, differentiation, and apoptosis. Recent studies have highlighted its role in regulating the Notch signaling pathway, which is crucial for developmental processes and cancer progression. NLE1 acts as an E3 ubiquitin ligase, tagging specific substrates for proteasomal degradation, thereby influencing cellular signaling and maintaining homeostasis. Given its involvement in critical regulatory pathways, researchers are increasingly focused on understanding the molecular mechanisms underlying NLE1 function and its potential implications in cancer biology and therapeutic interventions. The investigation of NLE1 recombinant protein provides a valuable tool for elucidating its structure-function relationship and discovering novel interactions with other cellular components. By generating and characterizing NLE1 in a recombinant form, scientists aim to explore its enzymatic activities and regulatory mechanisms in greater detail. This research not only enhances our understanding of NLE1’s role in normal cellular processes but also contributes to the development of targeted therapies for diseases wherein NLE1 dysregulation is implicated, thereby holding promise for advancements in cancer treatment strategies.
