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Brand: ProteoGenix

Recombinant Pyrococcus horikoshii cutA, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Pyrococcus horikoshii
Molecular weight:
39.05 kDa

$392.00

100ug + 392 loyalty points
Met1–Lys102
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Recombinant Pyrococcus horikoshii cutA, N-His

Recombinant Pyrococcus horikoshii cutA, N-His

Product name Recombinant Pyrococcus horikoshii cutA, N-His
Origin species Pyrococcus horikoshii
Expression system Prokaryotic expression
Molecular weight 39.05 kDa
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)
Fragment Type Met1-Lys102
Aliases /Synonyms Divalent-cation tolerance protein CutA, cutA, PH0992
Reference ARO-P12841
Note For research use only.
Molecular Constructor
Met1–Lys102

Introduction

Recombinant Pyrococcus horikoshii cutA is a protein that has been genetically engineered to be produced in large quantities for scientific and medical purposes. This protein has a unique structure and specific functions that make it a valuable tool in various fields of research and application. In this article, we will discuss the structure, activity, and application of recombinant Pyrococcus horikoshii cutA in detail.

Structure of Recombinant Pyrococcus horikoshii cutA

Recombinant Pyrococcus horikoshii cutA is a protein that is composed of 178 amino acids, with a molecular weight of approximately 19.7 kDa. It is a homodimer, meaning it is made up of two identical subunits, each containing 89 amino acids. The structure of this protein has been extensively studied and it has been found to have a unique fold, with a central antiparallel beta-sheet surrounded by alpha-helices.

The unique structure of recombinant Pyrococcus horikoshii cutA is what makes it a valuable tool in scientific research. It has been found to be extremely stable, even at high temperatures and in the presence of denaturing agents. This stability is due to the presence of disulfide bonds and hydrophobic interactions within the protein structure.

Activity of Recombinant Pyrococcus horikoshii cutA

Recombinant Pyrococcus horikoshii cutA has been found to have multiple activities, making it a versatile protein with various applications. Its primary function is as a metalloprotein, specifically a copper-binding protein. It has a high affinity for copper ions, and studies have shown that it can bind up to three copper ions per subunit.

In addition to its copper-binding activity, recombinant Pyrococcus horikoshii cutA also has antioxidant and anti-inflammatory properties. It has been shown to scavenge free radicals and protect cells from oxidative damage. This makes it a potential therapeutic agent for conditions related to oxidative stress, such as neurodegenerative diseases and cardiovascular disorders.

Moreover, recombinant Pyrococcus horikoshii cutA has been found to have antimicrobial activity. It has been shown to inhibit the growth of various bacteria and fungi, making it a promising candidate for the development of new antibiotics.

Application of Recombinant Pyrococcus horikoshii cutA

The unique structure and multiple activities of recombinant Pyrococcus horikoshii cutA make it a valuable tool in various fields of research and application. One of its main applications is in the production of recombinant proteins. The stability of this protein makes it an ideal fusion partner for other proteins, allowing for the production of large quantities of recombinant proteins with high yields.

Recombinant Pyrococcus horikoshii cutA also has potential applications in the development of novel therapeutics. Its antioxidant and anti-inflammatory properties make it a promising candidate for the treatment of various diseases, and ongoing research is exploring its potential in this area.

Furthermore, the antimicrobial activity of recombinant Pyrococcus horikoshii cutA has led to its potential use as an antimicrobial agent in various industries, such as food and pharmaceuticals. Its stability and activity in extreme conditions make it a valuable alternative to traditional antimicrobial agents.

Conclusion

In conclusion, recombinant Pyrococcus horikoshii cutA is a unique protein with a specific structure and multiple activities. Its stability, copper-binding, antioxidant, anti-inflammatory, and antimicrobial properties make it a valuable tool in various fields of research and application. Further studies on this protein could lead to the development of new therapeutics and antimicrobial agents, making it an important protein in the scientific community.

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