Analytical Data
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Gene name
SCO1
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简介
The SCO1 protein is a copper metal chaperone that contributes to the maturation of cytochrome c oxidase subunit II. SCO1 Protein, Human (GST) is the recombinant human-derived SCO1 protein, expressed by E. coli , with N-GST labeled tag.
- Application
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Alternative Names
Protein SCO1 Homolog Mitochondrial; SCO1; SCOD1
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Species
Human
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Source
E. coli
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Tag
N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75880
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Expression Region
G132-S301
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Protein Length
Partial
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Molecular Weight
20.40 kDa
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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
Related Products
Protein Description
SCO1 (SCO1 mitochondrial copper chaperone) is a critical protein involved in copper homeostasis within cells, particularly in mitochondria, where it plays a significant role in the maturation of cytochrome c oxidase, a key enzyme in the electron transport chain. Mutations in the SCO1 gene are associated with various mitochondrial diseases, notably those presenting with neurological defects and metabolic disorders. Research into the recombinant form of SCO1 has gained momentum as scientists aim to elucidate its functional mechanisms and interaction with copper ions and other mitochondrial proteins. By generating SCO1 as a recombinant protein in vitro, researchers can study its structure-function relationship, investigate its role in copper transfer, and validate its potential as a therapeutic target for mitochondrial-related pathologies. Understanding the intricate workings of SCO1 not only advances our knowledge of mitochondrial biology but also opens new avenues for the development of novel therapeutic strategies to combat diseases arising from mitochondrial dysfunctions. Consequently, SCO1 recombinant protein studies are pivotal in bridging gaps in our understanding of copper homeostasis and its implications for health and disease.
