Analytical Data
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Gene name
NFE2L2
- Application
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Alternative Names
NFE2L2;NRF2;Nuclear factor erythroid 2-related factor 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16236
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Expression Region
256-605aa
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AA Sequence
SILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN
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Molecular Weight
42.9 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
NFE2L2, also known as NRF2 (Nuclear Factor Erythroid 2-Related Factor 2), is a critical transcription factor that regulates the expression of antioxidant proteins and plays a pivotal role in cellular defense mechanisms against oxidative stress and inflammation. Its significance has garnered considerable attention in recent years, particularly in the context of various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. NFE2L2 modulates the expression of numerous genes involved in antioxidant response, xenobiotic metabolism, and cellular detoxification by binding to antioxidant response elements (AREs) in the promoter regions of target genes. Under normal conditions, NFE2L2 is kept in the cytoplasm by being bound to its inhibitor, KEAP1 (Kelch-like ECH-associated protein 1), which promotes its degradation. However, under oxidative stress, NFE2L2 dissociates from KEAP1, translocates to the nucleus, and activates the transcription of protective genes. This intriguing mechanism has stimulated research into NFE2L2 as a potential therapeutic target for enhancing antioxidant responses and combating oxidative damage. Investigating recombinant NFE2L2 protein offers insights into its structural properties, functional dynamics, and potential interactions with other cellular pathways. By utilizing recombinant techniques, researchers can produce ample quantities of NFE2L2 for biochemical assays, structural studies, and high-throughput screening of small molecules that modulate its activity. Understanding the role of NFE2L2 in cellular biology and its therapeutic potential could pave the way for novel prevention and treatment strategies for various diseases linked to oxidative stress and inflammation. Thus, the study of recombinant NFE2L2 represents a vital area of research with promising implications for health and disease management.
