Recombinant Mouse Nuclear Respiratory Factor 1 (NRF1) Protein (His-SUMO)

Name: Recombinant Mouse Nuclear Respiratory Factor 1 (NRF1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09514P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Nuclear Respiratory Factor 1 (NRF1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9WU00
Target Symbol	NRF1
Synonyms	Nrf1; Nuclear respiratory factor 1; NRF-1; Alpha palindromic-binding protein; Alpha-pal
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MEEHGVTQTEHMATIEAHAVAQQVQQVHVATYTEHSMLSADEDSPSSPEDTSYDDSDILNSTAADEVTAHLAAAGPVGMAAAAAVATGKKRKRPHVFESNPSIRKRQQTRLLRKLRATLDEYTTRVGQQAIVLCISPSKPNPVFKVFGAAPLENVVRKYKSMILEDLESALAEHAPAPQEVNSELPPLTIDGIPVSVDKMTQAQLRAFIPEMLKYSTGRGKPGWGKESCKPIWWPEDIPWANVRSDVRTEEQKQRVSWTQALRTIVKNCYKQHGREDLLYAFEDQQTQTQATTTHSIAHLVPSQTVVQTFSNPDGTVSLIQVGTGATVATLADASELPTTVTVAQVNYSAVADGEVEQNWATLQGGEMTIQTTQASEATQAVASLAEAAVAASQEMQQGATVTMALNSEAAAHAVATLAEATLQGGGQIVLSGETAAAVGALTGVQDANGLVQIPVSMYQTVVTSLAQGNGPVQVAMAPVTTRISDSAVTMDGQAVEVVTLEQ
Expression Range	1-503aa
Protein Length	Full Length
Mol. Weight	69.6kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Transcription factor that activates the expression of the EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key metabolic genes to cellular growth and development. Implicated in the control of nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication.
Subcellular Location	Nucleus.
Protein Families	NRF1/Ewg family
Database References	KEGG: mmu:18181 STRING: 10090.ENSMUSP00000065568 UniGene: Mm.259258
Tissue Specificity	Widely expressed in embryonic, fetal, and adult tissues.

Gene Functions References

mRNA and protein levels of Nrf1D were detected to varying extents in hemopoietic and somatic tissues. Nrf1D-derived isoforms were present in blood plasma. PMID: 30261697
Study identifies the endoplasmic reticulum (ER)-bound transcription factor nuclear factor erythroid 2 related factor-1, Nrf1/Nfe2L1, as a critical mediator of this process and shows that Nrf1 directly binds to and specifically senses cholesterol in the ER through a defined domain and that cholesterol regulates Nrf1 turnover, processing, localization, and activity. PMID: 29149604
data highlight a precise crosstalk between transcriptional regulation by NRF1 and epigenetic modulation during germ cell development and unequivocally demonstrate a novel role of NRF1 in spermatogenesis PMID: 28754714
Nrf1 knockdown suppressed the death of ubiquitin-deficient N2a cells upon exposure to As(III). Therefore, the levels of p65-Nrf1 may play an important role in the maintenance of cell viability under oxidative stress induced by As(III). PMID: 28237703
findings suggest that neurodegeneration in Nrf1 NKO mice may stem from the dysfunction of the ubiquitin-mediated regulation of neuronal proteins PMID: 28088524
Our findings demonstrate that DEE and a fraction derived from this extract exerts anti-inflammatory effects through Nrf2dependent HO-1 expression PMID: 26647788
NRF1 (nuclear respiratory factor 1) is a methylation-sensitive transcription factor; in the absence of DNA methylation, NRF1 binds to new sites and induces aberrant transcription PMID: 26675734
Nrf1 plays critical roles in regulating glucose metabolism, mitochondrial function, and insulin secretion, suggesting that Nrf1 may be a novel target to improve the function of insulin-secreting beta-cells. PMID: 25556857
lysine-specific demethylase 1 promotes oxidative phosphorylation in white adipose tissue, in cooperation with Nrf1. PMID: 24912735
Results show that Nrf1 may not be directly responsible for the loss of Nrf2-dependent inducibility of antioxidant and cytoprotective genes observed in aged animals. PMID: 24024152
Nrf1 controls both the fatty acid and the cystine/cysteine content of hepatocytes by participating in an elaborate regulatory network. PMID: 25092871
Data indicate both Nrf1a and Nrf1b isoforms transcripts were detected in different mouse and human cell lines, and in various mouse tissues. PMID: 23144760
During fetal myogenesis, Pitx2/3 control this redox state through the regulation of Nrf1 and of antioxidant pathways. PMID: 24871946
NST-adjoining TADs are partially repartitioned out of membranes into the cyto/nucleoplasmic side, where Nrf1 is subject to deglycosylation and/or proteolysis to generate 95-kDa and 85-kDa isoforms PMID: 23774320
NRF-2 and NRF-1 operate in a concurrent and parallel manner in mediating the tight coupling between energy metabolism and neuronal activity at the molecular level. PMID: 23085505
Nrf1 binds to the antioxidant response elements (AREs) in regulatory regions of the Lipin1 and PGC-1beta genes and the binding of Nrf1 to the AREs activates reporter gene transcription. PMID: 22586274
these results clearly suggest that both beta-TrCP- and Hrd1-dependent degradation mechanisms regulate the transcriptional activity of Nrf1 to maintain cellular homeostasis. PMID: 21911472
These results show that Nrf1 sustains the CNS homeostasis through regulating target genes distinct from those regulated by Nrf2. PMID: 21554501
Nrf1 is a key transcriptional regulator required for the expression of proteasomal genes in neurons and perturbations of Nrf1 function may contribute to the pathogenesis of neurodegenerative diseases PMID: 21536885
Study observed that Nrf1 overexpression stimulated cell proliferation, apoptosis, and cytokine expression. Prolonged Nrf1 induced an adipokine expression profile of insulin resistant adipocytes. PMID: 21053274
Findings indicate that TLR4-dependent NFkappaB and CREB activation co-regulate the NRF1 promoter with NFkappaB intronic enhancement and redox-regulated nuclear translocation, leading to downstream gene expression. PMID: 20587593
NRF-1 overexpression sensitizes cells to apoptosis on serum depletion PMID: 12533512
The Nrf1 metabolic pathway is the major regulator of genes that function in the mitochondrion. PMID: 12849846
NRF-1 and NRF-2 prove to be the two key bigenomic coordinators for transcriptional regulation of all cytochrome c oxidase subunits in neurons PMID: 18077450
beneficial effects of Sirt1 are due to at least two mechanisms: induction of antioxidant proteins MnSOD and Nrf1 PMID: 18599449
In this study they asked whether the interactions between USF1/USF2 and E-Box and Nrf1 and GC-Box in the brain of mouse are influenced by postnatal age and what link it has with reported age-related decrease in the expression of Fmr-1 gene. PMID: 18782566
Accumulation of nuclear NRF-1 protein leads to gene activation for heart mitochondrial biogenesis. PMID: 18845810
NRF-1 can also directly interact with poly(ADP-ribose) polymerase 1 (PARP-1) and co-purify the PARP-1.DNA-PK.Ku80.Ku70.topoisomerase IIbeta-containing protein complex. PMID: 19181665

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.