Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

TXNDC17 Human

Thioredoxin Domain Containing 17 Human Recombinant

Recombinant TXNDC17 protein, of human origin, is produced in E. coli. It is a single polypeptide chain comprising 147 amino acids (residues 1-123) with a molecular weight of 16.5kDa. The protein includes a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12881
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

TXNL1 Human

Thioredoxin-Like 1 Human Recombinant

Produced in E. coli, TXNL1 is a single, non-glycosylated polypeptide chain comprising 309 amino acids (specifically, amino acids 1 through 289). It possesses a molecular weight of 34.4 kDa. For purification purposes, a 20 amino acid His-tag is fused to the N-terminus of the protein, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT12967
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

TXNL4A Human

Thioredoxin-Like 4A Human Recombinant

Recombinant human TXNL4A, produced in E. coli, is a single polypeptide chain consisting of 166 amino acids (residues 1-142) with a molecular weight of 19.3 kDa. This protein includes a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13031
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

TXNL4B Human

Thioredoxin-Like 4B Human Recombinant

Produced in E. coli, TXNL4B is a single, non-glycosylated polypeptide chain with 185 amino acids (amino acids 1-149) and a molecular weight of 21.1 kDa. The protein is fused to a 36 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13125
Source
Escherichia Coli.
Appearance
A clear, sterile, and filtered solution.

TXN1 E.Coli

Thioredoxin E.Coli Recombinant

Recombinant Thioredoxin was expressed in E. coli and subsequently purified.
Shipped with Ice Packs
Cat. No.
BT12125
Source
Escherichia Coli.
Appearance
Sterile, dried powder obtained through lyophilization.

TXN1 Human

Thioredoxin Human Recombinant

Recombinant Human Thioredoxin, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 105 amino acids. It has a molecular weight of 11.7 kDa.
Shipped with Ice Packs
Cat. No.
BT12217
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TXN1 Human, His

Thioredoxin Human Recombinant, His Tag

Recombinant Human Thioredoxin, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 125 amino acids. The protein consists of the native sequence for human thioredoxin (105 amino acids) with an additional 20 amino acid His-tag fused at the N-terminus to facilitate purification. The molecular weight of the recombinant protein is approximately 13.9 kDa, though it may appear larger on SDS-PAGE due to the His-tag. The protein has been purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12306
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

TXNDC12 Human

Thioredoxin Domain Containing 12 Human Recombinant

Recombinant TXNDC12, expressed in E. coli, is a single polypeptide chain consisting of 184 amino acids (residues 27-172) with a molecular weight of 20.8 kDa. The protein is purified using proprietary chromatographic techniques and features an N-terminal 38 amino acid His-tag.
Shipped with Ice Packs
Cat. No.
BT12822
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

TXN1, His

Thioredoxin Recombinant, His Tag

Recombinant Thioredoxin, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 117 amino acids (specifically, amino acids 2-109) and possessing a molecular mass of 12.8 kDa. The protein features a 9 amino acid His Tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12597
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TXN2 Human

Thioredoxin-2 Human Recombinant

Recombinant MTRX, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 108 amino acids, resulting in a molecular weight of 11 kDa.
Shipped with Ice Packs
Cat. No.
BT12693
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
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 .

© Copyright 2024 Thebiotek. All Rights Reserved.