COX11, Cytochrome C Oxidase Copper Chaperone (COX10) Antibody

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Description
COX10 Antibody is a Rabbit Polyclonal Antibody against COX10.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | COX11, Cytochrome C Oxidase Copper Chaperone (COX10) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | ELISA: 1 µg/ml, WB: 1/500 - 1/2000. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified by affinity chromatography. |
| Size 1 | 20 µl |
| Size 2 | 100 µl |
| Size 3 | 2 × 100 µl |
| Form | Liquid |
| Tested Applications | ELISA, WB |
| Buffer | PBS, pH 7.3, containing 0.02% sodium azide, 50% glycerol. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q12887 |
| Gene ID | 1352 |
| NCBI Accession | NP_001294.2 |
| Background | Antibody anti-COX10 |
| Status | RUO |
| Note | Concentration: > 0.2 mg/ml - |
Descripción
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COX11, Cytochrome C Oxidase Copper Chaperone (COX10) Antibody
COX10 Antibody is a Rabbit Polyclonal Antibody against COX10.
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COX11, Cytochrome C Oxidase Copper Chaperone (COX10) Antibody
Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes heme A:farnesyltransferase, which is not a structural subunit but required for the expression of functional COX and functions in the maturation of the heme A prosthetic group of COX. This protein is predicted to contain 7-9 transmembrane domains localized in the mitochondrial inner membrane. A gene mutation, which results in the substitution of a lysine for an asparagine (N204K), is identified to be responsible for cytochrome c oxidase deficiency. In addition, this gene is disrupted in patients with CMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP (hereditary neuropathy with liability to pressure palsies) deletion.
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