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Brand: ProteoGenix

Recombinant Helicobacter pylori trxA/Thioredoxin

Host species:
Escherichia coli (E.coli)
Origin species:
Helicobacter pylori
Molecular weight:
0

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Recombinant Helicobacter pylori trxA/Thioredoxin

Recombinant Helicobacter pylori trxA/Thioredoxin

Product name Recombinant Helicobacter pylori trxA/Thioredoxin
Origin species Helicobacter pylori
Expression system Prokaryotic expression
Molecular weight 0
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Aliases /Synonyms Thioredoxin, Trx, rxA, HP_0824
Reference ARO-P12781
Note For research use only.

Introduction

Recombinant Helicobacter pylori trxA, also known as thioredoxin, is a protein that has been genetically engineered for use in scientific research and medical applications. This protein is derived from the bacterium Helicobacter pylori, which is a common cause of gastrointestinal diseases in humans. Recombinant trxA has been extensively studied and has shown promising potential in various fields, including diagnostics, therapeutics, and vaccine development.

Structure of Recombinant trxA

Recombinant trxA is a small protein consisting of 108 amino acids with a molecular weight of approximately 12 kDa. It is composed of two domains, the N-terminal domain (NTD) and the C-terminal domain (CTD), connected by a flexible linker region. The NTD contains the active site of trxA, which is a conserved cysteine residue that is responsible for its redox activity. The CTD, on the other hand, is involved in protein-protein interactions and is responsible for the stability of trxA.

Activity of Recombinant trxA

Recombinant trxA is a highly active protein with a variety of functions. Its primary role is to maintain the redox balance in the cell by reducing disulfide bonds in other proteins. This activity is essential for the proper folding and function of many proteins, making trxA a crucial player in cellular processes. In addition, trxA has been shown to have antioxidant properties and can protect cells from oxidative stress. Furthermore, trxA has been reported to have chaperone-like activity, assisting in the folding of newly synthesized proteins.

Application of Recombinant trxA

Recombinant trxA has numerous applications in both research and medicine. Its ability to maintain the redox balance in cells makes it a valuable tool for studying protein folding and function. Recombinant trxA has been used in various biochemical assays to study the activity of other proteins and enzymes. Additionally, trxA has been used as a fusion partner in protein expression systems, increasing the solubility and stability of target proteins.

In the medical field, recombinant trxA has shown potential as a diagnostic tool for Helicobacter pylori infection. Antibodies against trxA have been used in serological tests, and the protein itself has been used as an antigen in immunoassays. Furthermore, trxA has been investigated as a potential therapeutic target for Helicobacter pylori-related diseases. Studies have shown that inhibiting the activity of trxA can lead to the death of the bacterium, making it a promising target for new antibiotics.

Moreover, recombinant trxA has been explored as a vaccine candidate for Helicobacter pylori. As a highly conserved protein, trxA has the potential to induce a strong immune response, making it an attractive antigen for vaccine development. Studies have shown that immunization with recombinant trxA can elicit both humoral and cellular immune responses, providing protection against Helicobacter pylori infection in animal models.

Conclusion

Recombinant Helicobacter pylori trxA is a versatile protein with various applications in research and medicine. Its unique structure and activity make it a valuable tool for studying protein folding and function. In addition, trxA has shown potential as a diagnostic tool, a therapeutic target, and a vaccine candidate for Helicobacter pylori-related diseases. Further research on recombinant trxA is needed to fully understand its potential and to develop new and improved applications for this versatile protein.

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