Recombinant Human Cytochrome C Oxidase Subunit 1 (MT-CO1) Protein (His-GST)

Name: Recombinant Human Cytochrome C Oxidase Subunit 1 (MT-CO1) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-11033P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Cytochrome C Oxidase Subunit 1 (MT-CO1) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P00395
Target Symbol	MT-CO1
Synonyms	COI; COX I; COX1; COX1_HUMAN; COXI; Cytochrome c oxidase polypeptide I; Cytochrome c oxidase subunit 1; Cytochrome C Oxidase subunit I; Mitochondrially encoded cytochrome c oxidase I; MT CO1; MT-CO1; MTCO 1; MTCO1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	EAFASKRKVLMVEEPSMNLEWLYGCPPPYHTFEEPVYMKS
Expression Range	474-513aa
Protein Length	Partial
Mol. Weight	36.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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 subunit 2 and heme A of subunit 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.
Subcellular Location	Mitochondrion inner membrane; Multi-pass membrane protein.
Protein Families	Heme-copper respiratory oxidase family
Database References	HGNC: 7419 OMIM: 114500 KEGG: hsa:4512 STRING: 9606.ENSP00000354499
Associated Diseases	Leber hereditary optic neuropathy (LHON); Mitochondrial complex IV deficiency (MT-C4D); Recurrent myoglobinuria mitochondrial (RM-MT); Deafness, sensorineural, mitochondrial (DFNM); Colorectal cancer (CRC)

Gene Functions References

TGFbeta1 reduced complex IV protein MTCO1 abundance in both myoblasts and myotubes. PMID: 29335583
We investigated A5935G, G5949A, G6081A, G6267A mutations in MT-CO1 and T9540C in MT-CO3, and alterations detected during the analysis of MT-CO gene fragments in endometrial hyperplasia. Three new alterations detected in this study (A6052G, A9545G, G9575A) were described for the first time. PMID: 28819937
The monomeric COX1 assembly intermediate accumulates demonstrating a function of COX5A in complex IV biogenesis. A potential therapeutic lead is demonstrated by showing that copper supplementation leads to partial rescue of complex IV deficiency in patient fibroblasts. PMID: 28247525
High MTCO1 expression is associated with cognitive impairment in lung cancer. PMID: 26987334
patients with primary ovarian insufficiency exhibit an increased incidence of mitochondrial cytochrome c oxidase 1 gene mutations;MT-CO1 gene mutation may be causal in the disease PMID: 26225554
studies have provided mechanistic insights into crosstalk between assembly intermediates, import processes and the synthesis of COX subunits in mitochondria, thus linking conceptually separated functions. PMID: 25663696
The m.9267G>C MT-COIII mutation was present with a nonsynonymous inherited mitochondrial homoplasmic variation MT-COI m.5913 G>A. PMID: 25701779
A novel heteroplasmic mutation was identified in MTCO1, m.7402delC, causing frameshift and a premature termination codon in a mitochondrial encephalomyopathy patient with cytochrome c oxidase deficiency. PMID: 24956508
A novel m.6307A>G mutation in the mitochondrial COXI gene in asthenozoospermic infertile men. PMID: 23712756
mitochondrial DNA mutations in COI resulting in increased reactive oxygen and reactive nitrogen generation may be involved in prostate cancer biology PMID: 23509693
Possible association of a novel missense mutation A6375G in the mitochondrial cytochrome C oxidase I gene with asthenospermia in the Tunisian population PMID: 23030649
Abeta 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1 PMID: 22927926
Both full-length and truncated COX1 proteins physically interact with AFG3L2. PMID: 22252130
the possible role of m.7445 A>G in susceptibility to aminoglycoside induced-hearing loss PMID: 21621438
Data show that homoplasmic G6709A (MT-CO1) and G14804A (MT-CYB) alterations cause amino acid changes in the highly conserved residues. PMID: 21389643
MT-CO1 has a role in moderate mental retardation and a mild exercise intolerance [case report] PMID: 18484665
Screening of a Greek deafness population for the A7445G mitochondrial DNA COI mutation. PMID: 20382059
3 single nucleotide changes in 528 bp cytochrome oxidase gene fragment from 18 myelodysplastic syndrome patients were confirmed. PMID: 18718066
C6489A missense mutation in the mitochondrial DNA (mtDNA) CO I gene encoding the cytochrome c oxidase (COX) subunit I in a 17-year-old girl with epilepsia partialis continua PMID: 12140182
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
The expression of COX I subunits (I and III)was studied in blood platelets during aging. PMID: 14759509
High percentage of a 24.2 kb duplicated molecule was found in lymphocytes whereas the corresponding deletion dimer dominated in muscle. PMID: 15036329
A missense mutation within the mitochondrial cytochrome c oxidase I gene is associated with cancer. PMID: 16671096
Respiration dysfunction in cell with a mutation in COX I can be complementated by cell fusion with another cell carrying a mutation in cytochrome b. PMID: 16740593
Functional effects of nonsense mitochondrial DNA (mtDNA) mutations in the COXI and ND5 genes in a colorectal tumor cell line. PMID: 17341490
Cox-1 is expressed with a wide variety of levels and up-regulated significantly in endometrial cancer at the mRNA and protein levels, and may have an important role in tumor development in endometrial canceer. PMID: 18204294
the presence of one or more COI missense variants was not significantly associated with prostate cancer in African Americans PMID: 19267350
Trx2 overexpression modulates the mRNA levels of the COX1 (cytochrome oxidase subunit I) and Cytb (cytochrome b), which are known to be regulated by GR and NF-kappaB. PMID: 19570036

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.