COX4I1 Protein, Human (His-SUMO)
The COX4I1 protein is a component of cytochrome c oxidase, the final enzyme in the mitochondrial electron transport chain responsible for oxidative phosphorylation. COX4I1 Protein, Human (His-SUMO) is the recombinant human-derived COX4I1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
- Species: Human
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
Description
The COX4I1 protein is a component of cytochrome c oxidase, the final enzyme in the mitochondrial electron transport chain responsible for oxidative phosphorylation. COX4I1 Protein, Human (His-SUMO) is the recombinant human-derived COX4I1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
Background
COX4I1, a vital constituent of the cytochrome c oxidase, serves as a pivotal component in the mitochondrial electron transport chain, culminating in oxidative phosphorylation. This respiratory chain encompasses three multisubunit complexes—succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), and cytochrome c oxidase (complex IV, CIV)—that collaboratively facilitate the transfer of electrons from NADH and succinate to molecular oxygen. This intricate process generates an electrochemical gradient across the inner membrane, propelling transmembrane transport and fueling ATP synthase. Specifically, cytochrome c oxidase orchestrates the reduction of oxygen to water. The electron transfer from reduced cytochrome c in the intermembrane space involves intermediates, such as the dinuclear copper A center (CU(A)) in subunit 2 and heme A in subunit 1, ultimately converging at the active site in subunit 1—a binuclear center (BNC) comprised of heme A3 and copper B (CU(B)). The BNC efficiently reduces molecular oxygen to two water molecules, utilizing four electrons from cytochrome c in the intermembrane space and four protons from the mitochondrial matrix. COX4I1 thus plays a central role in energy metabolism, contributing to the intricate processes of oxidative phosphorylation.
Technical Parameters
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Species Human
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Source E. coli
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Tag N-6*His;N-SUMO
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Accession
P13073 (A23-K169)
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Molecular Construction
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N-term
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6*His-SUMO
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COX4I1 (A23-K169)
Accession # P13073 -
C-term
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Protein Length
Full Length of Mature Protein
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Synonyms
COX4I1; COX4-1; Prev. COX4; Cytochrome C Oxidase Subunit IV; Cytochrome C Oxidase Subunit 4 Isoform 1, Mitochondrial; COX IV-1; Cytochrome C Oxidase Subunit IV Isoform 1; Cytochrome C Oxidase Subunit 4; Cytochrome C Oxidase Polypeptide IV; MC4DN16; COXIV-
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AA Sequence
AHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK
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Predicted Molecular Mass
33.2 kDa
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US;may vary elsewhere.
Documentation
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)