Recombinant Human COX17 Protein, N-GST & C-His

Reference: YHG69801
Product nameRecombinant Human COX17 Protein, N-GST & C-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight32.98 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°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)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeLys21-Ile63
Aliases /SynonymsCytochrome c oxidase copper chaperone, COX17
ReferenceYHG69801
NoteFor research use only.

Description of Recombinant Human COX17 Protein, N-GST & C-His

Introduction

Recombinant Human COX17 Protein, also known as Cytochrome c oxidase copper chaperone, is a protein that plays a crucial role in cellular respiration. It is a small, highly conserved protein that is involved in the delivery of copper ions to the cytochrome c oxidase (COX) enzyme complex, which is responsible for the final step in the electron transport chain. In this article, we will explore the structure, activity, and applications of this important protein.

Structure of Recombinant Human COX17 Protein

Recombinant Human COX17 Protein is a small protein consisting of 69 amino acids with a molecular weight of approximately 7.8 kDa. It contains a conserved copper-binding motif, Cys-X-X-Cys, which is essential for its function as a copper chaperone. This motif is located at the C-terminus of the protein and is responsible for binding to copper ions.

The crystal structure of COX17 has been determined, revealing a compact structure with a beta-barrel fold. The copper-binding motif is located in a loop region, allowing for easy access to copper ions. The structure also contains two alpha-helices and two beta-strands, which are important for stabilizing the protein.

Activity of Recombinant Human COX17 Protein

The main function of Recombinant Human COX17 Protein is to deliver copper ions to the COX enzyme complex. Copper is an essential cofactor for COX, and without it, the enzyme cannot function properly. COX17 acts as a chaperone, binding to copper ions and delivering them to COX, where they are incorporated into the enzyme.

In addition to its role in copper delivery, COX17 has also been shown to have a cytoprotective function. It has been found to protect cells from oxidative stress by scavenging reactive oxygen species (ROS). This activity is independent of its role as a copper chaperone and is thought to be due to its ability to bind to iron ions.

Applications of Recombinant Human COX17 Protein

Recombinant Human COX17 Protein has a wide range of applications in both research and therapeutic settings. One of the main uses of this protein is in the study of cellular respiration and the electron transport chain. By studying the function of COX17, researchers can gain a better understanding of how cells produce energy and how disruptions in this process can lead to disease.

In addition, COX17 has been studied as a potential therapeutic target for diseases that involve mitochondrial dysfunction, such as Parkinson’s disease and amyotrophic lateral sclerosis (ALS). By targeting COX17, researchers hope to improve mitochondrial function and potentially slow the progression of these diseases.

Recombinant Human COX17 Protein is also used in the production of COX17 antibodies, which are important tools in studying the function and localization of this protein in cells. These antibodies can also be used for diagnostic purposes, such as detecting mutations in the COX17 gene that may be associated with mitochondrial diseases.

Conclusion

In summary, Recombinant Human COX17 Protein is a small but essential protein involved in copper delivery and cytoprotection. Its structure, activity, and applications make it a valuable tool in understanding cellular respiration and its role in diseases. Further research on this protein may lead to new therapeutic strategies for mitochondrial disorders and other diseases related to cellular respiration.

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