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NDUFS8 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O00217 |
|---|---|
| Clone Names | 101008222 |
| Gene ID | 4728 |
|---|---|
| Other Names | NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial, Complex I-23kD, CI-23kD, NADH-ubiquinone oxidoreductase 23 kDa subunit, TYKY subunit, NDUFS8 |
| 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 | NDUFS8 |
|---|---|
| Function | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:22499348). Essential for the catalytic activity and assembly of complex I (PubMed:22499348). |
| Cellular Location | Mitochondrion inner membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P42028}; Matrix side {ECO:0000250|UniProtKB:P42028} |
| Tissue Location | Expressed in all tissues with the highest level in heart and skeletal muscle and the lowest level in lung |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a subunit of mitochondrialNADH:ubiquinone oxidoreductase, or Complex I, a multimeric enzymeof the respiratory chain responsible for NADH oxidation, ubiquinonereduction, and the ejection of protons from mitochondria. Theencoded protein is involved in the binding of two of the six toeight iron-sulfur clusters of Complex I and, as such, is requiredin the electron transfer process. Mutations in this gene have beenassociated with Leigh syndrome.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Bourges, I., et al. Biochem. J. 383 (PT 3), 491-499 (2004) :Procaccio, V., et al. Neurology 62(10):1899-1901(2004)Ugalde, C., et al. Hum. Mol. Genet. 13(6):659-667(2004)Murray, J., et al. J. Biol. Chem. 278(39):37223-37230(2003)
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