Analytical Data
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Gene name
COX10
- Application
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Alternative Names
Protoheme IX farnesyltransferase. mitochondrial. EC:2.5.1.141. Heme O synthase
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8CFY5
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Expression Region
1-443aa
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AA Sequence
MAASPHTLSSRLLTGCVGGSVWYLERRTIQDSPHKFLHLLRNVNKQWITFQHFSFLKRMYVTQLNRSHNQQVRPKPEPVASPFLEKTSSGQAKAEIYEMRPLSPPSLSLSRKPNEKELIELEPDSVIEDSIDVGKETKEEKRWKEMKLQVYDLPGILAQLSKIKLTALVVSTTAAGFALAPGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRVALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDADRRSSRRLFFCSLWHLPLLLLLMLTCKRPSGGGDAGPPPS
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Molecular Weight
74.36 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
COX10 is a pivotal protein involved in the biosynthesis of heme a, an essential component of the cytochrome c oxidase (CCO), which is a key enzyme in the mitochondrial respiratory chain. The proper functioning of CCO is critical for cellular energy production through oxidative phosphorylation. Deficiencies in COX10 expression or function have been linked to various mitochondrial disorders, leading to impaired respiration and a plethora of metabolic diseases. Research on the recombinant expression of COX10 has gained attention as it offers insights into the mechanisms of mitochondrial dysfunction and potential therapeutic avenues. By producing recombinant COX10 protein in model systems, scientists can investigate its structure-function relationships, the effects of mutations, and the protein's interaction with other components of the respiratory chain. Moreover, understanding the cooperative interactions between COX10 and other mitochondrial proteins may facilitate drug development for mitochondrial diseases. The exploration of COX10's characteristics and its role in heme a synthesis may also contribute to advancements in biotechnological applications, including the design of novel bioenergetic therapies. Hence, COX10 serves as a critical focal point in both basic and applied biomedical research, driving the understanding of mitochondrial biology and its implications in health and disease.
