Recombinant Human Glutaredoxin 1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2268

Recombinant Human Glutaredoxin 1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2268
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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

Gene Functions References

  1. Glutaredoxin-1 silencing induces cell senescence via p53/p21/p16 signaling axis. PMID: 29356545
  2. 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
  3. 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
  4. Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes PMID: 28963348
  5. 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
  6. 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
  7. Glutaredoxin desensitizes lens to oxidative stress by connecting and integrating specific signaling and transcriptional regulation for antioxidant response. PMID: 27744453
  8. 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
  9. 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
  10. 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
  11. Glutaredoxin 1 protects human retinal pigment epithelial cells from oxidative damage by preventing AKT glutathionylation. PMID: 25788646
  12. A new function for GRX1 in neuronal copper homeostasis and in protection from copper-mediated oxidative injury. PMID: 24816595
  13. Human Grx1 can catalyse reduction of Atox1 by glutathione but only in the presence of Cu(I). PMID: 24522867
  14. Levels of GLRX in the cerebrospinal fluid increase significantly in the early stages of Alzheimer's disease. PMID: 24270206
  15. Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system. PMID: 24062305
  16. sputum glutaredoxin-1 may have a role in asthma, while protein S may have a role in better lung function PMID: 23370801
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. Role of glutaredoxin1 and glutathione in regulating the activity of the copper-transporting P-type ATPases, ATP7A and ATP7B. PMID: 20566629
  23. Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism PMID: 11832487
  24. Results suggest that glutaredoxin plays an important role during implantation, while Trx levels remained constant during the secretory phase. PMID: 12029072
  25. role of GRX in oxidative stress-induced signaling and cytotoxicity in glucose-deprived human cancer cells PMID: 12244106
  26. 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
  27. role in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1 PMID: 12723971
  28. secretion of Grx1 and its presence in plasma suggests extracellular functions as found for mammalian thioredoxin 1 PMID: 15184054
  29. Lung cells can synthesize Grx1 mRNA and protein. Grx1 is expressed in alveolar macrophages of healthy lung. PMID: 15297967
  30. 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
  31. Abeta neurotoxicity might be mediated by oxidation of GRX1 or TRX1 and subsequent activation of the ASK1 cascade. PMID: 16311508
  32. 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
  33. GRX plays an important role in PDGF-BB-dependent cell proliferation by regulating the redox state of LMW-PTP PMID: 16893901
  34. 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
  35. A novel mechanism of caspase-3 regulation by glutaredoxin is demonstrated in tumor necrosis factor-alpha-induced apoptosis. PMID: 17185628
  36. 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
  37. Deglutathionylation of IRF3 is necessary for efficient interaction of IRF3 with CREBBP. PMID: 18309294
  38. 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
  39. 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.

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

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