Recombinant Human Thioredoxin (TXN) Protein (His)

Name: Recombinant Human Thioredoxin (TXN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-05605P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Thioredoxin (TXN) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Uniprotkb	P10599
Target Symbol	TXN
Synonyms	ADF; ATL derived factor; ATL-derived factor; DKFZp686B1993; MGC61975; SASP; Surface associated sulphydryl protein; Surface-associated sulphydryl protein; testicular tissue protein Li 199; THIO_HUMAN; Thioredoxin; thioredoxin delta 3; TRDX; TRX 1; Trx; TRX1; TXN; TXN delta 3; TXN protein; zgc:92903
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Complete Sequence	MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
Expression Range	1-105aa
Protein Length	Full Length
Mol. Weight	13.9 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 20 mM PB, 150 mM NaCl, pH 7.2
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.

Target Details

Target Function	Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.; ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).
Subcellular Location	Nucleus. Cytoplasm. Secreted.
Protein Families	Thioredoxin family
Database References	HGNC: 12435 OMIM: 187700 KEGG: hsa:7295 STRING: 9606.ENSP00000363641 UniGene: PMID: 29348167 Based on recent research, it has been reported that the modulation of the Trx/TrxR system may be considered as a new target in the management of the metabolic syndrome, insulin resistance, and type 2 diabetes, as well as in the treatment of hypertension and atherosclerosis. In this review evidence about a possible role of this system as a marker of the metabolic syndrome is reported. [review] PMID: 29327078 By establishing that IL-4 is posttranslationally regulated by TRX-promoted reduction of a disulfide bond, our findings highlight a novel regulatory mechanism of the type 2 immune response that is specific to IL-4 over IL-13. PMID: 30104382 TRX1 is an actionable castration-resistant prostate cancer therapeutic target through its protection against AR-induced redox stress. PMID: 29089489 Trx-1 may be an important target for delaying oral malignant transformation, which provides a novel therapeutic strategy for the prevention and treatment of oral squamous cell carcinoma. PMID: 29328386 Results found the mRNA level of TRX-1 was significantly decreased (p<0.005), while the mRNA levels of TBP-2, COX-2, and TNF-alpha were significantly increased in the placentas in preeclampsia when compared to the normal group. PMID: 29999276 This study quantified the contribution of Trx reductase to the redox status of Trx, demonstrating that the redox profile of Trx is determined by the interplay between the elevation of intracellular redox potential and the reduction by Trx reductase and other endogenous molecules. PMID: 29509009 We identified a novel Jab1-Trx axis that is a key cellular process in the pathobiologic characteristics of acute myeloid leukemia (AML-M5). Targeting the ROS/Jab1/Trx pathway could be beneficial in the treatment of AML-M5 PMID: 28270496 study indicates that TRX levels cannot be used as a marker for Treatment Resistant Depression (trd) or repetitive transcranial magnetic stimulation treatment in TRD. In spite of this TRX levels have a positive correlation with language functions of the patients. PMID: 28442424 The reducing system of PTEN was comprised of NADPH, thioredoxin reductase (TrxR1), and thioredoxin (Trx). PMID: 28774816 Thioredoxin 1 modulates signaling mechanisms in the heart via its molecular targets, including transcription factors, microRNAs, histone deactylases, and protein kinases. (Review) PMID: 27993729 The ratio of thioredoxin/Keap1 protein level may be useful for suggesting distant metastasis in colorectal cancer. PMID: 29053012 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 Increased serum thioredoxin concentrations are highly associated with trauma severity PMID: 28347674 Plasma-TRX on day 1 was significantly increased in patients who later developed post-injury sepsis. In a logistic regression analysis including TRX, C-reactive protein, injury severity, massive transfusion, and admission blood pressure, TRX was the only variable independently associated with post-injury sepsis PMID: 28087409 High TRX1 expression is associated with myocardial infarction. PMID: 26933812 Data show that suberoylanilide hydroxamic acid (SAHA) induced apoptosis via the down-regulation thioredoxin1 (Trx1), which was regulated by microRNA miR-129-5p. PMID: 28667779 Analysis of 25 independent cohorts with 5910 patients showed that Trx1 and TrxR1 were both associated with a poor patient prognosis in terms of overall survival, distant metastasis free survival and disease free survival. PMID: 26760912 these findings demonstrate that Trx1 is a critical regulator of necroptosis that suppresses cell death by maintaining MLKL in a reduced inactive state. PMID: 28878015 Study shows that TRX1 and APEX1 expressions are up regulated in new Multiple Sclerosis (MS) patients compared to controls and might be implicated in pathogenesis of the disease. PMID: 28844667 CD40 activation resulted in down-regulation of Thioredoxin (Trx)-1 to permit ASK1 activation and apoptosis. Although soluble receptor agonist alone could not induce death, combinatorial treatment incorporating soluble CD40 agonist and pharmacological inhibition of Trx-1 was functionally equivalent to the signal triggered by mCD40L PMID: 27869172 our findings identify the TXN-FOXO1-p300 circuit as the sensor and effector of oxidative stress in DLBCL cells PMID: 27132507 Novel positive feedback loop between Trx-1 and S100P promotes colorectal cancer invasion and metastasis. PMID: 28483515 Thioredoxin attenuates oxidized low-density lipoprotein induced oxidative stress in human umbilical vein endothelial cells by reducing NOX2-NOX4 activity. PMID: 28688762 from the two catalytic cysteines of TRX1 the residue C32 is responsible for the high-affinity binding of TRX1 to the ASK1-TRX-binding domain in reducing conditions PMID: 27588831 findings suggest that the up-regulated RRM1 and hTrx1 in colorectal cancer directly interact with each other and promote RR activity, resulting in enhanced DNA synthesis and cancer malignancy. PMID: 28411237 Trx and its target proteins involved in redox signaling are critical for the control of cell fate such as cell survival and apoptosis [review] PMID: 27665998 herefore, the length of treatment with Nrf2 activators and/or Trx-1 has first to be studied in more detail in cardiovascular disorders. Moreover, a combination of Nrf2 activators and Trx-1 should be investigated and taken into consideration. PMID: 27923281 In an in vivo model of restenosis, which is characterized by oxidative stress, endothelial activation, and smooth muscle cell proliferation, Thioredoxin-1 protein levels are reduced in the endothelium of the carotids. APEX1 acts anti-apoptotic in endothelial cells. This anti-apoptotic effect depends on the first 20 amino acids of APEX1 PMID: 27835927 Authors found that TXN was under expressed in both AML and ALL groups as compared to the control group. Also TXN expression level was negatively correlated with serum 8-OHdG and tail moment in both AML and ALL. PMID: 27158980 Increased S-Trx and U-Trx concentrations, especially U-Trx/cr ratio, are closely associated with the severity of children hydronephrosis, substantializing Trx as a promising biomarker for the progression of children hydronephrosis PMID: 28111273 TRX in postoperative serum may be a potential biomarker to predict development of postoperative delirium and cognitive dysfunction in elderly patients undergoing hip fracture surgery. PMID: 28093200 Serum levels of thioredoxin and DJ-1 were significantly higher in non-small cell lung cancer patients; therefore, these may be utilized as novel diagnostic and prognostic biomarkers for non-small cell lung cancer PMID: 26334622 Elevated plasma thioredoxin levels are correlated with the severity and poor prognosis in subarachnoid hemorrhage patients. PMID: 27000227 Data show that the overexpression of thioredoxin1 (Trx1) attenuated apoptosis and reactive oxygen species (ROS) level in lung cancer cells. PMID: 26460805 Based on its collective anti-oxidative, cytoprotective, and cytokine-like properties of TRX, TRX is likely to be involved in the optimal growth and maturation of ovarian follicles and responsiveness to hyperstimulation. PMID: 26536897 change of serum levels of thioredoxin in patients with severe traumatic brain injury PMID: 26656445 Serum TRX levels at admission were associated with stroke severity and lesion volumes. PMID: 25520003 Results indicate that reduced Trx1 plays important protective roles against methyl methanesulfonate-induced DNA damage and cell death, suggesting that cell protection is regulated by the intracellular redox state. PMID: 26276860 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 differential expression in children with allergic asthma PMID: 25979194 identification of the novel interaction between Trx1 and AIF has provided opportunities to design and develop therapeutically relevant strategies that either promote or prevent this protein-protein interaction for the treatment of different disease PMID: 26119781 Thioredoxin 1 mediates TGF-beta-induced epithelial-mesenchymal transition in salivary adenoid cystic carcinoma. PMID: 26325518 In Jurkat cells exposed to ionizing radiatin (4 Gy), constitutively active Trx systems respond to restore cellular redox balance. After 16 hrs, Trx increases and rescues cells against IR-mediated damage. PMID: 26021764 genetic variants of TXN and COMT have roles in regulating abdominal obesity PMID: 26329592 Trx1 inhibition results in reactive oxygen species-induced apoptosis in Multiple myeloma cells, sensitizes Multiple myeloma cells to the NF-small ka, Cyrillicbeta inhibitors, and also induces apoptosis in bortezomib-resistant myeloma cells. PMID: 25945832 thioredoxin is a remote ischemic preconditioning-induced factor in heart tissue of cardiosurgical patients. PMID: 25622749 Plasma TRX levels of male patients in a manic episode were significantly lower than the controls. PMID: 25297388 the overexpression and nuclear translocation of thioredoxin-1 (Trx-1) are closely associated with hypoxia-drug resistance through the regulation of the metabolism by the oxidative stress response to glycolysis. PMID: 25656992 The crystal structure of fully oxidized thioredoxin shows a non-active Cys62-Cys69 disulfide bond in addition to the active Cys32-Cys35 disulfide. PMID: 26453009

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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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