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

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

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

COX4I1

Uniprot NO.

P13073

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

23-169

Target Protein Sequence

AHESVVKS EDFSLPAYMD RRDHPLPEVA HVKHLSASQK ALKEKEKASW SSLSMDEKVE LYRIKFKESF AEMNRGSNEW KTVVGGAMFF IGFTALVIMW QKHYVYGPLP QSFDKEWVAK QTKRMLDMKV NPIQGLASKW DYEKNEWKK
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 His-tagged/Tag-Free
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

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

In case of myocardial insufficiency and dilated cardiomyopathy, decreased expression of COX 4 results in an impaired CytOx activity. Higher enzymatic activity but equal oxygen consumption contribute to the pathophysiology of the myocardial insufficiency and appears as an indicator of oxidative stress. This kind of dysregulation should be in the focus for the development of diagnostic and therapy procedures PMID:30223867
COX4I1 variant K101N was identified in a patient with short stature, poor weight gain and increased chromosomal breaks, simulating Fanconi anemia. PMID:28766551
This cohort study showed that the COX411 gene was down regulation between patients with idiopathic Parkinson disease and controls PMID:28916538
We provide evidence that COX4-1 controls BMI1 expression via a redox mechanism PMID:25726526
COXIV mRNA (1.6 fold; P<0.01) and COXIV protein expression (1.5 fold; P<0.05) were increased by training but COXIV protein expression was decreased (20%; P<0.01) by acute exercise pre- and post-training. PMID:23285255
COX activity (electron transport complex IV) is reduced by 29% in maternal history of Alzheimer's disease compared to normal controls, and by 30% compared to paternal history of Alzheimer's disease. PMID:21841246
Studies suggest a model that links cell signaling with the phosphorylation state of Cytochrome c (Cytc) and cytochrome c oxidase (COX). PMID:21771582
Studies suggest that the main function of nuclear encoded subunits of cytochrome c oxidase appears to be "only" to control the activity of the mitochondrial subunits. PMID:21802404
Studies indicate that the mechanism for proton pumping in cytochrome c oxidase is based on an electrostatic analysis of a kinetic experiment for the O to E transition. PMID:21978537
Studies indicate that nitric oxide (NO) inhibition of cytochrome c oxidase (CcOX) is rapid and reversible and may occur in competition with oxygen. PMID:21939634
Studies indicate that the cytochrome oxidase enzyme-substrate (ES) Michaelis complex of cell respiration, the dioxygen adduct of heme a(3), which he termed Compound A. PMID:22079200
Novel insights into the assembly and function of human nuclear-encoded cytochrome c oxidase subunits 4 PMID:20307258
Data found that subunits Cox6a, Cox6b and Cox7a assembled into pre-existing complex IV, while Cox4-1 and Cox6c subunits assembled into subcomplexes that may represent rate-limiting intermediates. PMID:19843159
study points to a role for surfeit 1(SURF1) in promoting the association of cytochrome c oxidase II with the cytochrome c oxidase I.cytochrome c oxidase subunit 4.cytochrome c oxidase subunit 5A subassembly PMID:14607829
Under conditions of reduced oxygen availability, hypoxia-inducible factor 1 reciprocally regulates COX4 subunit expression by activating transcription of the genes encoding COX4-2 and LON, a mitochondrial protease that is required for COX4-1 degradation. PMID:17418790