NFE2L2 Human

Nuclear Factor Erythroid 2-Like 2 Human Recombinant
Cat. No.
BT29248
Source
Escherichia Coli.
Synonyms
NFE2L2, Nuclear factor erythroid 2-related factor 2, NF-E2-related factor 2, NFE2-related factor 2, HEBP1, Nuclear factor, erythroid derived 2, like 2, NRF2.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NFE2L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 625 amino acids (1-605 a.a) and having a molecular mass of 69.9kDa.
NFE2L2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Nuclear factor (erythroid-derived 2)-like 2 (NRF2), also known as NFE2L2, is a transcription factor that plays a crucial role in the cellular response to oxidative stress. It belongs to the basic leucine zipper (bZIP) family and forms heterodimers with small Maf proteins to bind to Maf recognition elements (MAREs). NRF2 also interacts with the antioxidant response element (ARE) to regulate the expression of genes involved in detoxification and antioxidant defense. Widely expressed across various tissues, NRF2 is primarily located in the cytoplasm under normal conditions. Upon exposure to oxidative stress or electrophilic compounds, NRF2 dissociates from its cytoplasmic repressor Keap1 and translocates to the nucleus, where it activates the transcription of target genes.
Description
This product consists of the recombinant human NFE2L2 protein, produced in E. coli. It is a single, non-glycosylated polypeptide chain encompassing 625 amino acids (specifically, residues 1 to 605). The protein has a molecular weight of 69.9 kDa. For purification and detection purposes, a 20-amino acid His-tag is fused to the N-terminus. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
The product is a clear solution that has been sterilized through filtration.
Formulation
The NFE2L2 protein is provided in a solution with a concentration of 0.25 mg/ml. The solution is buffered with phosphate-buffered saline (PBS) at a pH of 7.4 and contains 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product should be kept refrigerated at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, adding a carrier protein like HSA or BSA (0.1%) is advisable. It is important to avoid repeated freeze-thaw cycles to maintain product integrity.
Purity
The purity of the NFE2L2 protein is greater than 85%, as determined by SDS-PAGE analysis.
Synonyms
NFE2L2, Nuclear factor erythroid 2-related factor 2, NF-E2-related factor 2, NFE2-related factor 2, HEBP1, Nuclear factor, erythroid derived 2, like 2, NRF2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRRKEYELEK QKKLEKERQE QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIQSETSGSA NYSQVAHIPK SDALYFDDCM QLLAQTFPFV DDNEVSSATF QSLVPDIPGH IESPVFIATN QAQSPETSVA QVAPVDLDGM QQDIEQVWEE LLSIPELQCL NIENDKLVET TMVPSPEAKL TEVDNYHFYS SIPSMEKEVG NCSPHFLNAF EDSFSSILST EDPNQLTVNS LNSDATVNTD FGDEFYSAFI AEPSISNSMP SPATLSHSLS ELLNGPIDVS DLSLCKAFNQ NHPESTAEFN DSDSGISLNT SPSVASPEHS VESSSYGDTL LGLSDSEVEE LDSAPGSVKQ NGPKTPVHSS GDMVQPLSPS QGQSTHVHDA QCENTPEKEL PVSPGHRKTP FTKDKHSSRL EAHLTRDELR AKALHIPFPV EKIINLPVVD FNEMMSKEQF NEAQLALIRD IRRRGKNKVA AQNCRKRKLE NIVELEQDLD HLKDEKEKLL KEKGENDKSL HLLKKQLSTL YLEVFSMLRD EDGKPYSPSE YSLQQTRDGN VFLVPKSKKP DVKKN.

Product Science Overview

Structure and Function

NRF2 is a basic leucine zipper (bZIP) protein that binds to antioxidant response elements (AREs) in the promoter regions of genes encoding cytoprotective proteins . This binding induces the expression of various genes involved in the cellular response to oxidative stress, including phase II detoxifying enzymes . NRF2 is known to inhibit the NLRP3 inflammasome, which is involved in the inflammatory response .

The structure of NRF2 includes seven highly conserved domains known as NRF2-ECH homology (Neh) domains . These domains are responsible for various functions:

  • Neh1: Allows heterodimerization with small Maf proteins.
  • Neh2: Binds to the cytosolic repressor Keap1.
  • Neh3: Plays a role in protein stability and acts as a transactivation domain.
  • Neh4 and Neh5: Act as transactivation domains, binding to cAMP Response Element Binding Protein (CREB).
  • Neh6: Contains a degron involved in the degradation of NRF2, even under stressed conditions .
Role in Disease and Therapeutic Potential

NRF2 is involved in a complex regulatory network that affects metabolism, inflammation, autophagy, proteostasis, mitochondrial physiology, and immune responses . Due to its role in protecting cells from oxidative stress, NRF2 is a promising therapeutic target for diseases caused by oxidative damage, such as neurodegenerative diseases, cardiovascular diseases, and cancer .

Several drugs that stimulate the NFE2L2 pathway are currently being studied for their potential to treat these conditions . The ability of NRF2 to regulate the expression of cytoprotective genes makes it a valuable target for developing new therapeutic strategies.

Research and Applications

In vitro studies have shown that NRF2 binds to AREs in the promoter regions of genes encoding cytoprotective proteins, leading to the upregulation of these genes . This has significant implications for developing treatments that can enhance the body’s natural defense mechanisms against oxidative stress.

Human recombinant NRF2 is used in research to study its effects on gene expression and its potential therapeutic applications. By understanding how NRF2 functions and regulates gene expression, researchers can develop new strategies to combat diseases associated with oxidative stress.

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