Recombinant Human Glutaredoxin 1 Protein (His Tag)

Name: Recombinant Human Glutaredoxin 1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2268
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P35754
Synonym	GLRX, GRX, GRX1
Background	Glutaredoxin-1, also known as GRX1 and GLRX, belongs to theglutaredoxin family. Glutaredoxinsare smallredoxenzymes that useglutathioneas a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. Glutaredoxin-1 functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Glutaredoxin-1 exists in either a reduced or an oxidized form. Glutaredoxins function as electron carriers in the glutathione-dependent synthesis ofdeoxyribonucleotidesby the enzymeribonucleotide reductase.
Description	A DNA sequence encoding the human GLRX (P35754)(Met1-Gln106) was expressed with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	His
AA Sequence	Met1-Gln106
Molecular Weight	The recombinant human GLRX consists of 121 a.a. and predicts a molecular mass of 13.6 KDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
Purity	>85% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tirs, 10% Glycerol, 1mM DTT, pH 8.0..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular Location	Cytoplasm.
Protein Families	Glutaredoxin family
Database References	HGNC: 4330 OMIM: 600443 KEGG: hsa:2745 STRING: 9606.ENSP00000237858 UniGene: Hs.28988

Gene Functions References

Glutaredoxin-1 silencing induces cell senescence via p53/p21/p16 signaling axis. PMID: 29356545
Overexpression of NOS3 increased the levels and activities of proteins of the redoxin systems, Trx1, Grx1, TrxR1 and TxnIP, and the levels of signaling proteins (Akt1, pAkt1(-)Ser473, MapK, pMapK, Stat3, Fas). PMID: 28162284
Based on the roGFP2-hGrx1 signals, glutathione-dependent redox potentials of -267mV and -328mV, respectively, were obtained. Employing these novel tools, initial studies on the effects of redox-active agents and clinically employed antimalarial drugs were carried out on both organelles. PMID: 28062360
Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes PMID: 28963348
GRX1 overexpression constrains oxidative stress and apoptosis in osteoarthritis chondrocytes by regulating CREB/HO-1, providing a novel insight into the molecular mechanism and potential treatment of osteoarthritis. PMID: 28843170
Our results indicate that Grx1 upregulation promotes neuroinflammation and consequent neuronal cell death in vitro, and synergizes with proinflammatory insults to promote DA loss in vivo. PMID: 27224303
Glutaredoxin desensitizes lens to oxidative stress by connecting and integrating specific signaling and transcriptional regulation for antioxidant response. PMID: 27744453
Glrx ablation stabilizes HIF-1alpha by increasing GSH adducts on Cys(520) promoting in vivo HIF-1alpha stabilization, VEGF-A production, and revascularization in the ischemic muscles. PMID: 27162359
The results demonstrate that the antiproliferative effect of NO is hampered by Trx1 and Grx1 and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies. PMID: 26210445
Prx2 glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling. GSH/Grx1 provide an alternative mechanism to thioredoxin and thioredoxin reductase for Prx2 recycling. PMID: 26601956
Glutaredoxin 1 protects human retinal pigment epithelial cells from oxidative damage by preventing AKT glutathionylation. PMID: 25788646
A new function for GRX1 in neuronal copper homeostasis and in protection from copper-mediated oxidative injury. PMID: 24816595
Human Grx1 can catalyse reduction of Atox1 by glutathione but only in the presence of Cu(I). PMID: 24522867
Levels of GLRX in the cerebrospinal fluid increase significantly in the early stages of Alzheimer's disease. PMID: 24270206
Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system. PMID: 24062305
sputum glutaredoxin-1 may have a role in asthma, while protein S may have a role in better lung function PMID: 23370801
Studies show that the glutaredoxin system with glutathione plays a backup role to keep oxidized thioredoxin 1 (Trx1) reduced in cells with loss of thioredoxin reductase 1 (TrxR1) activity. PMID: 22977247
Data show that glutaredoxin acts as a reductant for methionine sulfoxide reductases A and B (MsrA and MsrB) with or without resolving cysteine. PMID: 22634633
These results showed that cigarette smoke can modulate glutaredoxin 1, not only at the expression level, but can also directly modify glutaredoxin 1 itself, decreasing its activity. PMID: 21454804
Microsecond-millisecond motions in glutaredoxin result from substrate binding and not from crossing of the transition state energy barrier of product formation. Instead substrate binding induces a conformational change. PMID: 21323311
findings reveal another signalling molecule affected by S-glutathionylation and uncover a crucial role for GRX-1 in the TRAF6-dependent activation of NF-kappaB by IL-1R/TLRs. PMID: 21078302
Role of glutaredoxin1 and glutathione in regulating the activity of the copper-transporting P-type ATPases, ATP7A and ATP7B. PMID: 20566629
Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism PMID: 11832487
Results suggest that glutaredoxin plays an important role during implantation, while Trx levels remained constant during the secretory phase. PMID: 12029072
role of GRX in oxidative stress-induced signaling and cytotoxicity in glucose-deprived human cancer cells PMID: 12244106
facilitates GS-radical scavenging and S-glutathionylation of redox signal mediators, consistent with a critical role in redox signal transduction and cellular regulation PMID: 12556467
role in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1 PMID: 12723971
secretion of Grx1 and its presence in plasma suggests extracellular functions as found for mammalian thioredoxin 1 PMID: 15184054
Lung cells can synthesize Grx1 mRNA and protein. Grx1 is expressed in alveolar macrophages of healthy lung. PMID: 15297967
Grx1(as) cDNA is an alternatively spliced human Grx1 cDNA and the Grx1(as) 3'-untranslated region may have a role in stabilizing mRNA PMID: 15637068
Abeta neurotoxicity might be mediated by oxidation of GRX1 or TRX1 and subsequent activation of the ASK1 cascade. PMID: 16311508
We propose that GRX1 is essential for ATPase function and catalyses either the reduction of intramolecular disulphide bonds or the deglutathionylation of the cysteine residues within the CxxC motifs to facilitate copper-binding for subsequent transport. PMID: 16884690
GRX plays an important role in PDGF-BB-dependent cell proliferation by regulating the redox state of LMW-PTP PMID: 16893901
Grx1 is a potential redox modulatory protein regulating the intracellular as well as extracellular homeostasis of glutathionylated proteins and GSH in human lung. PMID: 17064412
A novel mechanism of caspase-3 regulation by glutaredoxin is demonstrated in tumor necrosis factor-alpha-induced apoptosis. PMID: 17185628
In this review, reversible glutathiolation of procaspase-3 by glutaredoxin provides further mechanistic insight into the role of reactive oxygen species in TNF-alpha-induced apoptosis. PMID: 17272816
Deglutathionylation of IRF3 is necessary for efficient interaction of IRF3 with CREBBP. PMID: 18309294
downregulation of Grx1 leads to mitochondrial dysfunction through oxidative modification of the outer membrane protein, VDAC, providing support for the critical role of Grx1 in maintenance of mitochondrial membrane potential PMID: 18560520
NO increased the S-glutathiolation of SERCA, and adenoviral overexpression of glutaredoxin-1 prevented both the HNO-stimulated oxidative modification of SERCA and its activation. PMID: 19265039

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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.

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