1. Search Result
Search Result
Results for "

thioredoxin

" in MedChemExpress (MCE) Product Catalog:

36

Inhibitors & Agonists

7

Fluorescent Dye

1

Biochemical Assay Reagents

3

Peptides

1

Natural
Products

24

Recombinant Proteins

1

Isotope-Labeled Compounds

10

Antibodies

Cat. No. Compare Product Name Species Source
  • HY-P73431

    thioredoxin; TXN; Trx; ADF; TRX1; SASP

    Human E. coli
    Thioredoxin/TXN protein participates in multiple redox reactions, utilizing its active center dithiol for reversible oxidation and disulfide bond formation. It catalyzes important dithiol-disulfide exchange and plays a key role in S-nitrosylation of cysteine residues in response to intracellular nitric oxide. Thioredoxin/TXN Protein, Human (Solution) is the recombinant human-derived Thioredoxin/TXN protein, expressed by E. coli , with tag free. The total length of Thioredoxin/TXN Protein, Human (Solution) is 105 a.a., with molecular weight of ~14 kDa.
  • HY-P73431A

    thioredoxin; TXN; Trx; ADF; TRX1; SASP

    Human E. coli
    Thioredoxin/TXN Protein participates in diverse redox reactions, using its active center dithiol for reversible oxidation and disulfide bond formation. It catalyzes crucial dithiol-disulfide exchanges and plays a pivotal role in S-nitrosylation of cysteine residues, responding to intracellular nitric oxide. Thioredoxin regulates caspase-3 activity by nitrosylating CASP3's active site cysteine. It also influences FOS/JUN AP-1 DNA binding and augments interleukin-2 receptor expression, showcasing its multifaceted cellular role beyond redox regulation. Thioredoxin/TXN Protein, Human is the recombinant human-derived Thioredoxin/TXN protein, expressed by E. coli, with tag free. The total length of Thioredoxin/TXN Protein, Human is 105 a.a., with molecular weight of ~14 kDa.
  • HY-P73432A

    thioredoxin; TXN; Trx; ADF; TRX1; SASP

    Mouse E. coli
    Thioredoxin/TRX Protein engages in diverse redox reactions, utilizing its active dithiol center for reversible oxidation and disulfide formation. It catalyzes essential dithiol-disulfide exchanges and plays a crucial role in S-nitrosylation of cysteine residues, responding to intracellular nitric oxide. Thioredoxin inhibits CASP3 activity by nitrosylating its active site cysteine. It also regulates FOS/JUN AP-1 DNA binding activity and influences interleukin-2 receptor expression, showcasing its multifaceted cellular role beyond redox regulation. Thioredoxin/TRX Protein, Mouse (N-His) is the recombinant mouse-derived Thioredoxin/TRX protein, expressed by E. coli, with N-6*His labeled tag. The total length of Thioredoxin/TRX Protein, Mouse (N-His) is 105 a.a., with molecular weight of ~15 kDa.
  • HY-P73432

    thioredoxin; TXN; Trx; ADF; TRX1; SASP

    Mouse E. coli
    Thioredoxin/TRX proteins participate in multiple redox reactions, utilizing their reactive dithiol centers for reversible oxidation and disulfide bond formation. It catalyzes important dithiol-disulfide exchange and plays a key role in S-nitrosylation of cysteine residues in response to intracellular nitric oxide. Thioredoxin/TRX Protein, Mouse is the recombinant mouse-derived Thioredoxin/TRX protein, expressed by E. coli , with tag free. The total length of Thioredoxin/TRX Protein, Mouse is 105 a.a., with molecular weight of ~15 kDa.
  • HY-P71496

    trxA; fipA; tsnC; b3781; JW5856; thioredoxin 1; Trx-1

    E.coli E. coli
    Thioredoxin-1/TRXA Protein participates in diverse redox reactions, facilitating reversible oxidation of its active center dithiol to form a disulfide bond and catalyzing critical dithiol-disulfide exchanges. Operating as a monomer, Thioredoxin-1 exhibits versatility in redox functions and interacts with bacteriophage T3 DNA polymerase, suggesting broader involvement in molecular processes beyond its primary redox activities. Thioredoxin-1/TRXA Protein, E.coli (His) is the recombinant E. coli-derived Thioredoxin-1/TRXA protein, expressed by E. coli , with N-His labeled tag. The total length of Thioredoxin-1/TRXA Protein, E.coli (His) is 108 a.a., with molecular weight of ~15.7 kDa.
  • HY-P71393

    thioredoxin Mitochondrial; MTRX; Mt-Trx; thioredoxin-2; TXN2; TRX2

    Human E. coli
    As a monomer, the TXN2 protein is critical for maintaining mitochondrial reactive oxygen species (ROS) homeostasis, regulating apoptosis, and ensuring cell viability. Its unique dithiol reducing activity fine-tunes cellular redox balance, making a significant contribution to overall cellular health. TXN2 Protein, Human (His) is the recombinant human-derived TXN2 protein, expressed by E. coli , with tag free. The total length of TXN2 Protein, Human (His) is 107 a.a., with molecular weight of ~13 kDa.
  • HY-P77258

    thioredoxin reductase 1, cytoplasmic; GRIM-12; thioredoxin reductase TR1; TR; KDRF

    Human E. coli
    The homodimeric flavoprotein TRXR1/TXNRD1 plays a key role in cellular redox regulation, growth and differentiation. It reduces the disulfide protein thioredoxin (Trx) to its dithiol-containing form and exhibits reductase activity towards hydrogen peroxide (H2O2). TRXR1/TXNRD1 Protein, Human (His) is the recombinant human-derived TRXR1/TXNRD1 protein, expressed by E. coli , with N-His labeled tag. The total length of TRXR1/TXNRD1 Protein, Human (His) is 487 a.a., with molecular weight of ~55 kDa.
  • HY-P77258A

    thioredoxin reductase 1, cytoplasmic; GRIM-12; thioredoxin reductase TR1; TR; KDRF

    Human E. coli
    The homodimeric flavoprotein TRXR1/TXNRD1 plays a key role in cellular redox regulation, growth and differentiation. It reduces the disulfide protein thioredoxin (Trx) to its dithiol-containing form and exhibits reductase activity towards hydrogen peroxide (H2O2). TRXR1/TXNRD1 Protein, Human (N-His) is the recombinant human-derived TRXR1/TXNRD1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of TRXR1/TXNRD1 Protein, Human (N-His) is 487 a.a., with molecular weight of ~60 kDa.
  • HY-P7422

    rHuthioredoxin/TXN, His; Trx; ADF; TRX1

    Human E. coli
    Thioredoxin/TXN Protein, Human (His) is a thiol-oxidoreductase enzyme which control cellular redox homeostasis.
  • HY-P71371

    thioredoxin-related transmembrane protein 2; Cell proliferation-inducing gene 26 protein; thioredoxin domain-containing protein 14; TMX2

    Human E. coli
    The TMX2 protein is an endoplasmic reticulum- and mitochondria-associated regulator that controls cellular redox status and affects post-translational modifications, protein folding, and mitochondrial activity. TMX2 Protein, Human (His) is the recombinant human-derived TMX2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of TMX2 Protein, Human (His) is 172 a.a., with molecular weight of ~23.0 kDa.
  • HY-P71232
    PRDX4 Protein, Human (His)
    1 Publications Verification

    Peroxiredoxin-4; Antioxidant Enzyme AOE372; AOE37-2; Peroxiredoxin IV; Prx-IV; thioredoxin Peroxidase AO372; thioredoxin-Dependent Peroxide Reductase A0372; PRDX4

    Human E. coli
    PRDX4, a thiol-specific peroxidase, enzymatically reduces hydrogen peroxide and organic hydroperoxides, crucial for cellular protection. It detoxifies peroxides, acts as a sensor for hydrogen peroxide-mediated signaling, and contributes to NF-kappa-B activation regulation. PRDX4's multifaceted activity underscores its significance in cellular redox homeostasis and potential impact on intracellular signaling. PRDX4 Protein, Human (His) is the recombinant human-derived PRDX4 protein, expressed by E. coli , with N-6*His labeled tag. The total length of PRDX4 Protein, Human (His) is 234 a.a., with molecular weight of 27-30 kDa.
  • HY-P7802

    rEcothioredoxin/TXN, His; Trx; ADF; TRX1

    E.coli E. coli
    Thioredoxin/TXN Protein, E.coli (His) is a hydrogen carrier protein and exists widely in organism. Thioredoxin suppression disbalances insulin responsiveness in chicken cardiomyocytes through PI3K/Akt pathway inhibition.
  • HY-P71231
    PRDX1 Protein, Human (His)
    1 Publications Verification

    Peroxiredoxin-1; Natural killer cell-enhancing factor A; NKEF-A; Proliferation-associated gene protein; PAG; thioredoxin peroxidase 2; thioredoxin-dependent peroxide reductase 2; PAGA; PAGB; TDPX2

    Human E. coli
    Peroxiredoxin-1 (PRDX1) is a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides and plays a crucial role in cellular protection against oxidative stress. It detoxifies peroxide and senses hydrogen peroxide-mediated signaling events. PRDX1 Protein, Human (His) is the recombinant human-derived PRDX1 protein, expressed by E. coli , with C-6*His, N-6*His labeled tag. The total length of PRDX1 Protein, Human (His) is 199 a.a., with molecular weight of ~27.0 kDa.
  • HY-P76681

    thioredoxin-related transmembrane protein 1; TMX; TXNDC; TXNDC1

    Human HEK293
    TMX1 Protein is a member of the protein disulfide isomerase (PDI) family and is a transmembrane thiol isomerase. TMX1 Protein can participate in various redox reactions, reversibly oxidizes to disulfide through its active center thiol, and catalyzes the thiol-disulfide exchange reaction. In addition, TMX1 Protein negatively regulates the activation of αibβ3 integrin and platelet aggregation outside the cell. TMX1 Protein, Human (HEK293, Fc) is the recombinant human-derived TMX1 protein, expressed by HEK293 , with C-mFc labeled tag. The total length of TMX1 Protein, Human (HEK293, Fc) is 154 a.a., with molecular weight of ~44.4 kDa.
  • HY-P77270

    thioredoxin-like protein 4B; Dim1-like protein; DIM2; DLP

    Human E. coli
    TXNL4B Protein, vital for pre-mRNA splicing, is crucial for S/G(2) cell cycle transition, forming homodimers and interacting with the U5-102 kDa spliceosome subunit. It plays a key role in splicing intricacies and influences cell cycle dynamics. TXNL4B Protein, Human (His) is the recombinant human-derived TXNL4B protein, expressed by E. coli , with N-His labeled tag. The total length of TXNL4B Protein, Human (His) is 149 a.a., with molecular weight of ~19 kDa.
  • HY-P77268

    thioredoxin domain-containing protein 17; TRP14; Protein 42-9-9; TXNL5

    Human E. coli
    TXNDC17 Protein is a novel 14-kDa disul-fide reductase of the TXN (thioredoxin) family. It has peroxidase activity and protein-disulfide reductase (NAD(P)) activity. TXNDC17 is involved in the TNF (tumor necrosis factor) signaling pathway. And it inhibits the pathways of NF-κB, mitogen-activated protein kinases, and apoptosis in cells stimulated with TNF-alpha. Furthermore, TXNDC17 is an efficient S-denitrosylase. TXNDC17 Protein, Human is the recombinant human-derived TXNDC17 protein, expressed by E. coli , with tag free. The total length of TXNDC17 Protein, Human is 123 a.a., with molecular weight of ~13.9 kDa.
  • HY-P77269

    thioredoxin-like protein 4A; DIM1 protein homolog; DIM1; TXNL4

    Human E. coli
    The TXNL4A protein plays a key role in pre-mRNA splicing and is an important component of U5 snRNP, U4/U6-U5 tri-snRNP complex, and precatalytic spliceosome (spliceosome B complex). It contributes to spliceosome assembly and is an integral part of the complex process of spliceosome function. TXNL4A Protein, Human (His) is the recombinant human-derived TXNL4A protein, expressed by E. coli , with N-His labeled tag. The total length of TXNL4A Protein, Human (His) is 142 a.a., with molecular weight of ~14 kDa.
  • HY-P71146

    Peroxiredoxin-5; PRDX5; Alu corepressor 1; Antioxidant enzyme B166; AOEB166; Liver tissue 2D-page spot 71B; PLP; Peroxiredoxin V; Prx-V; Peroxisomal antioxidant enzyme; TPx type VI; thioredoxin peroxidase PMP20; thioredoxin reductase

    Human HEK293
    The PRDX5 protein (or Peroxiredoxin-5) plays a critical role as a thiol-specific peroxidase that reduces hydrogen peroxide and organic hydroperoxides. This enzyme activity is essential for cells to defend against oxidative stress and detoxify peroxides. PRDX5/Peroxiredoxin-5 Protein, Human (HEK293, His) is the recombinant human-derived PRDX5/Peroxiredoxin-5 protein, expressed by HEK293 , with N-6*His labeled tag. The total length of PRDX5/Peroxiredoxin-5 Protein, Human (HEK293, His) is 162 a.a., with molecular weight of ~17.0 kDa.
  • HY-P71394

    thioredoxin domain-containing protein 15; C5orf14; UNQ335/PRO534

    Human HEK293
    TXNDC15 Protein positively regulates ciliary hedgehog signaling, crucial in cellular communication. It actively participates in ciliogenesis, contributing to the structural and functional dynamics of the cellular organelle. TXNDC15 Protein, Human (HEK293, His) is the recombinant human-derived TXNDC15 protein, expressed by HEK293, with C-6*His labeled tag. The total length of TXNDC15 Protein, Human (HEK293, His) is 289 a.a., with molecular weight of 50-60 kDa.
  • HY-P70901

    thioredoxin domain-containing protein 4; ER protein 44; KIAA0573; TXNDC4

    Human HEK293
    The TXNDC4 protein is critical in cellular processes, mediating thiol-dependent retention in the early secretory pathway. Its conserved CRFS motif forms mixed disulfide bonds with substrate proteins to control oxidative protein folding in the endoplasmic reticulum and maintain cellular redox balance. TXNDC4 Protein, Human (HEK293, His) is the recombinant human-derived TXNDC4 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of TXNDC4 Protein, Human (HEK293, His) is 373 a.a., with molecular weight of ~50.0 kDa.
  • HY-P71046

    thioredoxin Domain-Containing Protein 12; Endoplasmic Reticulum Resident Protein 18; ER Protein 18; ERp18; Endoplasmic Reticulum Resident Protein 19; ER Protein 19; ERp19; thioredoxin-Like Protein p19; hTLP19; TXNDC12; TLP19

    Human HEK293
    The TXNDC12 protein is an important endoplasmic reticulum-localized protein disulfide bond reductase that plays a key role in promoting disulfide bond formation in client proteins. As an essential component of cellular machinery, TXNDC12 contributes to complex protein folding processes, highlighting its importance in maintaining correct protein structure and function. TXNDC12 Protein, Human (HEK293, His) is the recombinant human-derived TXNDC12 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of TXNDC12 Protein, Human (HEK293, His) is 142 a.a., with molecular weight of ~18.0 kDa.
  • HY-P71464

    Epididymis secretory sperm binding protein Li 2a; HEL S 2a; MGC4104; Natural killer cell enhancing factor B; Natural killer cell-enhancing factor B; Natural Killer Enhancing Factor B; NKEF B; NKEF-B; NKEFB; Peroxiredoxin 2; Peroxiredoxin-2; PRDX 2; PRDX2; PrP; PRX2; PRXII; PTX1; TDPX1; Thiol Specific Antioxidant 1 ; Thiol specific antioxidant protein; Thiol-specific antioxidant protein; thioredoxin Dependent Peroxide Reductase 1; thioredoxin peroxidase 1; thioredoxin-dependent peroxide reductase 1; Torin; TPX1; TSA

    Human E. coli
    Peroxiredoxin-2 (PRDX2) is a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides, which is essential for cellular protection against oxidative stress. It detoxifies peroxide, senses hydrogen peroxide-mediated signaling events, and may participate in signaling cascades initiated by growth factors and tumor necrosis factor-alpha. Peroxiredoxin-2/PRDX2 Protein, Human (His) is the recombinant human-derived Peroxiredoxin-2/PRDX2 protein, expressed by E. coli , with N-His labeled tag. The total length of Peroxiredoxin-2/PRDX2 Protein, Human (His) is 197 a.a., with molecular weight of ~25.8 kDa.
  • HY-P71147

    thioredoxin-Dependent Peroxide Reductase Mitochondrial; Antioxidant Protein 1; AOP-1; HBC189; Peroxiredoxin III; Prx-III; Peroxiredoxin-3; Protein MER5 homolog; PRDX3; AOP1

    Human E. coli
    The PRDX3 protein is a thiol-specific peroxidase that plays a key role in cellular defense by reducing hydrogen peroxide and organic hydroperoxides to water and alcohols. It detoxifies peroxides and cooperates with MAP3K13 to regulate NF-kappa-B activation. PRDX3 Protein, Human is the recombinant human-derived PRDX3 protein, expressed by E. coli , with tag free. The total length of PRDX3 Protein, Human is 194 a.a., with molecular weight of ~25.0 kDa.
  • HY-P71193

    Protein Disulfide-Isomerase A6; Endoplasmic Reticulum Protein 5; ER Protein 5; ERp5; Protein Disulfide Isomerase P5; thioredoxin Domain-Containing Protein 7; PDIA6; ERP5; P5; TXNDC7

    Human HEK293
    PDIA6 protein has molecular chaperone activity, which can inhibit the aggregation of misfolded proteins and contribute to quality control. It negatively regulates the unfolded protein response (UPR) by binding to ERN1 and inhibiting its signaling. PDIA6 Protein, Human (HEK293, His) is the recombinant human-derived PDIA6 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of PDIA6 Protein, Human (HEK293, His) is 421 a.a., with molecular weight of ~52.0 kDa.

Inquiry Online

Your information is safe with us. * Required Fields.

Salutation

 

Country or Region *

Applicant Name *

 

Organization Name *

Department *

     

Email Address *

 

Product Name *

Cat. No.

 

Requested quantity *

Phone Number *

     

Remarks

Inquiry Online

Inquiry Information

Product Name:
Cat. No.:
Quantity:
MCE Japan Authorized Agent: