Recombinant Macaca fascicularis Cytochrome c oxidase subunit 2 (MT-CO2)
Description
Introduction to Recombinant Macaca fascicularis Cytochrome c Oxidase Subunit 2 (MT-CO2)
Recombinant Macaca fascicularis Cytochrome c oxidase subunit 2 (MT-CO2) is a recombinant protein derived from the crab-eating macaque, a species of macaque commonly used in biomedical research. This protein is part of the cytochrome c oxidase complex, which plays a crucial role in the electron transport chain during oxidative phosphorylation in mitochondria. The MT-CO2 subunit is encoded by the mitochondrial gene MT-CO2 and is essential for the proper functioning of the enzyme, facilitating the transfer of electrons to oxygen and contributing to ATP production.
Structure and Function
The recombinant MT-CO2 protein from Macaca fascicularis is a full-length protein consisting of 227 amino acids. It is typically expressed in E. coli and may be tagged with various affinity tags to facilitate purification. The structure of MT-CO2 includes several key domains that are crucial for its interaction with other subunits of cytochrome c oxidase and for its enzymatic activity.
| Protein Characteristics | Description |
|---|---|
| Species | Macaca fascicularis (Crab-eating macaque) |
| Gene Name | MT-CO2 |
| Protein Length | 227 amino acids |
| Expression System | E. coli |
| Tag Type | Determined during production |
| Storage Buffer | Tris-based buffer, 50% glycerol |
Research Applications
Recombinant MT-CO2 from Macaca fascicularis is used in various research applications, including studies on mitochondrial function, oxidative phosphorylation, and neurodegenerative diseases. The protein can be used in ELISA assays to detect antibodies against MT-CO2 or to study protein-protein interactions.
ELISA Assays
ELISA kits for recombinant Macaca fascicularis MT-CO2 are available, allowing researchers to quantify the protein or antibodies against it in samples. These assays are useful for studying immune responses or for detecting MT-CO2 in biological samples.
| ELISA Kit Details | Description |
|---|---|
| Quantity | 50 µg (other quantities available upon request) |
| Product Type | Recombinant Protein |
| Species | Macaca fascicularis |
| Uniprot Number | P11948 |
| Storage Conditions | -20°C or -80°C for extended storage |
Mitochondrial Disorders
Mitochondrial disorders often result from mutations in genes encoding components of the electron transport chain, including cytochrome c oxidase. These disorders can lead to a range of clinical symptoms, including muscle weakness, neurological deficits, and metabolic disturbances.
Neurodegenerative Diseases
Mitochondrial dysfunction is implicated in the pathogenesis of neurodegenerative diseases such as Parkinson's disease and Alzheimer's disease. Research on mitochondrial proteins like MT-CO2 can provide insights into the mechanisms underlying these diseases and potential therapeutic strategies.
Product Specs
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The tag type will be determined during the production process. If you require a specific tag, please inform us, and we will prioritize its development.
Target Background
Q&A
Basic Research Questions
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What is Cytochrome c Oxidase Subunit 2 (MT-CO2) and what is its significance in Macaca fascicularis?
Cytochrome c oxidase subunit 2 (MT-CO2) is one of the three mitochondrial DNA (mtDNA) encoded subunits of respiratory complex IV. In Macaca fascicularis (crab-eating macaque), as in other mammals, MT-CO2 plays a crucial role in the electron transport chain of oxidative phosphorylation. This protein contains a binuclear copper A center (CuA) that receives electrons from cytochrome c and transfers them to the catalytic center of the enzyme . The significance of studying MT-CO2 in M. fascicularis lies in its evolutionary conservation and its potential as a model for human mitochondrial function and pathologies.
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How does MT-CO2 function within the mitochondrial respiratory chain?
MT-CO2 functions as an integral component of cytochrome c oxidase (Complex IV), which represents the terminal complex of the electron transport chain. Methodologically, the process operates as follows:
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Electrons originate from reduced cytochrome c in the intermembrane space
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These electrons are transferred via the dinuclear copper A center (CuA) of MT-CO2
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The electrons then move through heme A of subunit 1 to the active site
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At the binuclear center formed by heme A3 and copper B (CuB), molecular oxygen is reduced to water
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This process utilizes 4 electrons from cytochrome c and 4 protons from the mitochondrial matrix
This electron transfer contributes to the electrochemical gradient that drives ATP synthesis, forming the basis of cellular energy production.
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What are the structural characteristics of recombinant MT-CO2 from Macaca fascicularis?
Recombinant M. fascicularis MT-CO2 typically consists of 227 amino acids with a molecular weight of approximately 25.6 kDa . The structure includes:
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An N-terminal domain containing two transmembrane alpha-helices
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A conserved cysteine loop at positions 196 and 200, which forms part of the CuA center
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A conserved histidine at position 204 that also contributes to the CuA center
When expressed as a recombinant protein, MT-CO2 is often tagged (commonly with His-tag) to facilitate purification and detection in experimental settings .
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