Recombinant Human Glutaredoxin-1 (GLRX) Protein (GST)

Name: Recombinant Human Glutaredoxin-1 (GLRX) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-10069P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Glutaredoxin-1 (GLRX) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P35754
Target Symbol	GLRX
Synonyms	GLRX; Glrx1; GLRX1_HUMAN; Glutaredoxin; Glutaredoxin-1; Glutaredoxin1; Grx 1; Grx; Grx1; MGC117407; Thioltransferase 1; Thioltransferase; Thioltransferase-1; Thioltransferase1; TTase ; TTase 1; TTase-1; TTase1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ
Expression Range	1-106aa
Protein Length	Full Length
Mol. Weight	38.8kDa
Research Area	Transport
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	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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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.

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