Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

TXN Mouse

Thioredoxin Mouse Recombinant

TXN Mouse  Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a.) and having a molecular mass of 14.1kDa. TXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT12018
Source

Escherichia Coli.

Appearance

Sterile filtered colorless solution.

TXN1 E.Coli

Thioredoxin E.Coli Recombinant

Recombinant Thioredoxin was purified from E. coli harboring its gene.
Shipped with Ice Packs
Cat. No.
BT12125
Source
Escherichia Coli.
Appearance
Sterile Lyophilized Powder.

TXN1 Human

Thioredoxin Human Recombinant

Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.
Shipped with Ice Packs
Cat. No.
BT12217
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

TXN1 Human, His

Thioredoxin Human Recombinant, His Tag

Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Shipped with Ice Packs
Cat. No.
BT12306
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

TXN1, His

Thioredoxin Recombinant, His Tag

Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT12597
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

TXN2 Human

Thioredoxin-2 Human Recombinant

MTRX Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 108 amino acids and having a molecular mass of 11 kDa.
Shipped with Ice Packs
Cat. No.
BT12693
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

TXN2 Yeast

Thioredoxin-2 Yeast Recombinant

Thioredoxin-2 Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 12.6kDa.

Shipped with Ice Packs
Cat. No.
BT12765
Source
Escherichia Coli.
Appearance
Sterile Lyophilized Powder.

TXNDC12 Human

Thioredoxin Domain Containing 12 Human Recombinant

TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.
TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12822
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TXNDC17 Human

Thioredoxin Domain Containing 17 Human Recombinant

TXNDC17 Human Recombinant produced in E. coli is a single polypeptide chain containing 147 amino acids (1-123) and having a molecular mass of 16.5kDa.
TXNDC17 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12881
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TXNL1 Human

Thioredoxin-Like 1 Human Recombinant

TXNL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-289.a.a) and having a molecular mass of 34.4kDa.
TXNL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12967
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
Definition and Classification

Thioredoxin is a class of small redox proteins found in nearly all known organisms. These proteins play a crucial role in many biological processes, including redox signaling. In humans, thioredoxins are encoded by the TXN and TXN2 genes . Thioredoxin proteins are characterized by a conserved active site containing two cysteine residues in a CXXC motif, which are essential for their redox activity .

Biological Properties

Thioredoxins are ubiquitously expressed in various tissues and are essential for life in mammals . They are involved in maintaining redox homeostasis, cell proliferation, and DNA synthesis . Thioredoxin-1 (Trx-1) is found in the cytoplasm and nucleus, while Thioredoxin-2 (Trx-2) is located in the mitochondria . These proteins are also present in plants, where they regulate functions such as photosynthesis, growth, and development .

Biological Functions

The primary function of thioredoxin is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds . Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase . They play a significant role in immune responses and pathogen recognition by modulating the expression of defense-related genes . In plants, thioredoxins contribute to defense responses against pathogens by regulating the expression of pathogenesis-related genes .

Modes of Action

Thioredoxins interact with a broad range of proteins through a redox mechanism based on the reversible oxidation of cysteine thiol groups to disulfides . This interaction involves the transfer of two electrons and two protons, resulting in the covalent interconversion of a disulfide and a dithiol . Thioredoxins are maintained in their reduced state by the enzyme thioredoxin reductase, which uses NADPH as a co-substrate . This system is crucial for maintaining cellular redox homeostasis and protecting cells from oxidative damage .

Regulatory Mechanisms

The expression and activity of thioredoxins are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Thioredoxin expression can be induced by oxidative stress, UV irradiation, and inflammatory cytokines . Post-translational modifications, such as phosphorylation and acetylation, also play a role in modulating thioredoxin activity .

Applications

Thioredoxins have significant applications in biomedical research, diagnostic tools, and therapeutic strategies . They are used as biomarkers for oxidative stress and inflammation . In cancer therapy, targeting the thioredoxin system has shown promise in inhibiting tumor growth and enhancing the efficacy of chemotherapeutic agents . Additionally, thioredoxins are being explored as potential therapeutic agents for treating diseases associated with oxidative stress .

Role in the Life Cycle

Thioredoxins play a vital role throughout the life cycle, from development to aging and disease . During development, they are essential for cell proliferation and differentiation . In aging, thioredoxins help mitigate oxidative damage and maintain cellular function . In diseases such as cancer and chronic obstructive pulmonary disease (COPD), thioredoxins contribute to disease progression by regulating redox homeostasis and inflammation .

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