Product Details

Purity

>85% (SDS-PAGE)

Target Names

COX1

Uniprot No.

P00401

Alternative Names

COX1; OXI3; Q0045Cytochrome c oxidase subunit 1; EC 1.9.3.1; Cytochrome c oxidase polypeptide I

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

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.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

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.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

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

Datasheet

Please contact us to get it.

Target Background

Function

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 COX2 and heme A of COX1 to the active site in COX1, 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 (Probable). COX1 is a catalytic core subunit containing heme A and the active site BNC with heme A3 and the copper atom CU(B).

Gene References into Functions

results indicate that the Cox1 C-terminal end is a key regulator of CcO biogenesis and that it is important for supercomplex formation/stability. PMID: 28490636
Data indicate the paramagnetic relaxation enhancements (PRE) on cytochrome c peroxidase (CcP) caused by its partner cytochrome c (Cc) carrying a spin label. PMID: 24726731
COX-deficient mitochondria activate Ras on their outer membrane that establishes a pro-ROS accumulation environment by suppressing antioxidant defenses and the ERAD-mediated turnover of the ER-localized NADPH oxidase Yno1p. PMID: 23931758
COX is assembled from separate assembly modules, each containing one of the mitochondrial-translated core subunits in association with a unique set of nuclear-encoded subunits PMID: 23897805
a novel activity of Pet54 required for normal synthesis of Cox1 that is independent of the Cox1 C-terminal end. PMID: 20807763
show that the two heme a cofactor sites in Cox1 form downstream of Mss51- and Coa1-containing Cox1 intermediates. PMID: 19995914
The mutant Cox10 complex has enhanced efficiency in the addition of heme a to Cox1. PMID: 19841065
mRNA translation in mitochondria prevented by overexpression of Pet111 PMID: 15916616
Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assemb PMID: 17882260
The matrix-localized Coa2 protein may aid in stabilizing an early Cox1 intermediate containing the nuclear subunits Cox5a and Cox6. PMID: 18541668
Ccm1p/Ygr150cp is essential to remove the fourth intron of COX1 pre-mRNAs in Saccaromyces cerevisiae. PMID: 19562342

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Subcellular Location

Mitochondrion inner membrane; Multi-pass membrane protein.

Protein Families

Heme-copper respiratory oxidase family

Database Links

KEGG: sce:Q0045

STRING: 4932.Q0045

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Recombinant Saccharomyces cerevisiae Cytochrome c oxidase subunit 1 (COX1), partial

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