Analytical Data
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Gene name
CYC1
- Application
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Alternative Names
Complex III subunit 4Complex III subunit IVCytochrome b-c1 complex subunit 4Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit ;Cytochrome c-1
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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
P08574
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Expression Region
85-325aa
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Molecular Weight
54.4 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
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Protein Description
CYC1, or Cytochrome c1, is a crucial component of the mitochondrial electron transport chain, playing a significant role in cellular respiration and energy production. The study of CYC1 recombinant proteins has gained prominence due to their potential applications in biochemistry and therapeutics. Researchers focus on characterizing the structure and function of CYC1 to understand its involvement in various metabolic processes and its implications in diseases, particularly those related to mitochondrial dysfunction. Expression of recombinant CYC1 proteins allows for the detailed analysis of its enzymatic properties and interactions with other mitochondrial components. Advances in techniques such as site-directed mutagenesis and high-resolution spectroscopy have facilitated the exploration of CYC1's role in redox reactions and its impact on electron transfer efficiency. Additionally, the study of CYC1 in the context of recombinant protein technology holds promise for developing novel bioengineering applications, including the design of biofuel cells and therapeutic agents targeting mitochondrial diseases. Understanding the properties and mechanisms of CYC1 can lead to significant insights into mitochondrial biology and potential strategies for disease intervention, emphasizing the importance of this research in the fields of molecular biology and biotechnology.
