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Recombinant Bovine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (COX4I1)

Recombinant Bovine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (COX4I1)

Code: CSB-CF005832BO

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20μg100μg

US$3594

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Express system: in vitro E.coli expression system

Species: Bos taurus (Bovine)

Tag Info: N-terminal 10xHis-tagged

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Product Details
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Target Background

Product Details

Target Names

COX4I1

Uniprot NO.

P00423

Alternative Names

COX4I1; COX4; Cytochrome c oxidase subunit 4 isoform 1, mitochondrial; Cytochrome c oxidase polypeptide IV; Cytochrome c oxidase subunit IV isoform 1; COX IV-1

Species

Bos taurus (Bovine)

Source

in vitro E.coli expression system

Expression Region

23-169

Target Protein Sequence

AHGSVVKSEDYALPSYVDRRDYPLPDVAHVKNLSASQKALKEKEKASWSSLSIDEKVELY RLKFKESFAEMNRSTNEWKTVVGAAMFFIGFTALLLIWEKHYVYGPIPHTFEEEWVAKQT KRMLDMKVAPIQGFSAKWDYDKNEWKK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 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 cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunbit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.

Gene References into Functions

Structure of bovine cytochrome c oxidase crystallized at a neutral pH has been reported. PMID:28695851
Studies indicate that the patterns of charge translocation of cytochrome c oxidase coupled to transfer of the 3rd and 4th electrons are very similar. PMID:21889506
Studies indicate that time-resolved resonance Raman (RR) spectroscopy of whole mitochondria identified a band at 571cm(-1) arising from the oxygenated intermediate at Deltat=0.4, 0.6 and 1.4ms. PMID:22172733
Studies indicate that mutational amino acid replacement in proton channels, at the negative (N) side of membrane-inserted prokaryotic aa(3) oxidases, as well as Zn(2+) binding at this site in the bovine oxidase, uncouples proton pumping. PMID:22100820
Studies indicate that nitric oxide (NO) binding to reduced ba(3) and bovine cytochrome aa3. PMID:22201543
Studies indicate that X-ray structure of heart cytochrome c oxidase (CcO) suggest that O(2) molecules are transiently trapped at the Cu(B) site before binding to Fe(a3)(2+) to provide O(2)(-). PMID:22236806
Studies indicate that photoexcitation of Ru (II) to Ru(II*) leads to rapid electron transfer to the ferric heme group in cytochrome c (Cc), followed by electron transfer to Cu(A) in cytochrome c oxidase (CcO) with a rate constant of 60,000s(-1). PMID:21939635
Studies suggest that the master-equation models address the question of how pumping can be achieved in a system in which all reaction steps are reversible. PMID:21946020
Studies suggest for the His291 model of proton pumping in cytochrome c oxidase (CcO). PMID:22086149