Analytical Data
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Gene name
COX5b
- Application
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Alternative Names
COXVB; Cytochrome c oxidase subunit 5B, mitochondrial
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10606
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Expression Region
Ala32~His129
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Molecular Weight
16kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Cox5b is a crucial subunit of the cytochrome c oxidase (COX) complex, which plays a vital role in the mitochondrial respiratory chain and energy metabolism. This reconstituted protein has garnered significant interest in recent years due to its involvement in various physiological and pathological processes, including cellular respiration, oxidative stress response, and apoptosis. Research has shown that alterations in the expression and function of Cox5b can contribute to mitochondrial dysfunction, a hallmark of many diseases such as neurodegenerative disorders, cardiovascular diseases, and cancer. Given that COX is the terminal enzyme in the electron transport chain, understanding the structural and functional properties of Cox5b is essential for elucidating its role in energy production and potential implications in disease mechanisms. Moreover, reconstituted Cox5b proteins are valuable tools for studying the interactions within the COX complex and developing therapeutic strategies aimed at restoring normal mitochondrial function. Recent advancements in molecular biology techniques have enabled the expression and purification of Cox5b, facilitating in-depth studies of its biochemical properties and its interactions with other mitochondrial components, thereby providing insights into its regulatory roles and potential as a therapeutic target.
