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COX10 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q12887 |
|---|---|
| Clone Names | 90921008 |
| Gene ID | 1352 |
|---|---|
| Other Names | Protoheme IX farnesyltransferase, mitochondrial, 251-, Heme O synthase, COX10 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | COX10 |
|---|---|
| Function | Converts protoheme IX and farnesyl diphosphate to heme O. |
| Cellular Location | Mitochondrion membrane; Multi-pass membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
Cytochrome c oxidase (COX), the terminal component of themitochondrial respiratory chain, catalyzes the electron transferfrom reduced cytochrome c to oxygen. This component is aheteromeric complex consisting of 3 catalytic subunits encoded bymitochondrial genes and multiple structural subunits encoded bynuclear genes. The mitochondrially-encoded subunits function inelectron transfer, and the nuclear-encoded subunits may function inthe regulation and assembly of the complex. This nuclear geneencodes heme A:farnesyltransferase, which is not a structuralsubunit but required for the expression of functional COX andfunctions in the maturation of the heme A prosthetic group of COX.This protein is predicted to contain 7-9 transmembrane domainslocalized 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 oxidasedeficiency. In addition, this gene is disrupted in patients withCMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP(hereditary neuropathy with liability to pressure palsies)deletion.
References
Chen, Z., et al. Oncogene 29(30):4362-4368(2010)Vitali, M., et al. J Neural Transm 116(12):1635-1641(2009)Dassa, E.P., et al. EMBO Mol Med 1(1):30-36(2009)Veluthakal, R., et al. Diabetes 56(1):204-210(2007)Coenen, M.J., et al. Ann. Neurol. 56(4):560-564(2004)
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