NDUFV1 Antibody(N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P49821 |
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Clone Names | 100623327 |
Gene ID | 4723 |
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Other Names | NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial, Complex I-51kD, CI-51kD, NADH dehydrogenase flavoprotein 1, NADH-ubiquinone oxidoreductase 51 kDa subunit, NDUFV1, UQOR1 |
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 | NDUFV1 (HGNC:7716) |
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Synonyms | UQOR1 |
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:28844695). Part of the peripheral arm of the enzyme, where the electrons from NADH are accepted by flavin mononucleotide (FMN) and then passed along a chain of iron-sulfur clusters by electron tunnelling to the final acceptor ubiquinone (PubMed:28844695). Contains FMN, which is the initial electron acceptor as well as one iron-sulfur cluster (PubMed:28844695). |
Cellular Location | Mitochondrion inner membrane {ECO:0000250|UniProtKB:P25708}; Peripheral membrane protein {ECO:0000250|UniProtKB:P25708}; Matrix side {ECO:0000250|UniProtKB:P25708} |
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Background
The mitochondrial respiratory chain provides energy tocells via oxidative phosphorylation and consists of fourmembrane-bound electron-transporting protein complexes (I-IV) andan ATP synthase (complex V). This gene encodes a 51 kDa subunit ofthe NADH:ubiquinone oxidoreductase complex I; a large complex withat least 45 nuclear and mitochondrial encoded subunits thatliberates electrons from NADH and channels them to ubiquinone. Thissubunit carries the NADH-binding site as well as flavinmononucleotide (FMN)- and Fe-S-biding sites. Defects in complex Iare a common cause of mitochondrial dysfunction; a syndrome thatoccurs in approximately 1 in 10,000 live births. Mitochondrialcomplex I deficiency is linked to myopathies, encephalomyopathies,and neurodegenerative disorders such as Parkinson's disease andLeigh syndrome. Alternative splicing results in multiple transcriptvariants encoding distinct isoforms.
References
Wang, W., et al. Nucleic Acids Res. (2010) In press :Moran, M., et al. Biochim. Biophys. Acta 1802(5):443-453(2010)Saito, A., et al. J. Hum. Genet. 54(6):317-323(2009)Starr, J.M., et al. Mech. Ageing Dev. 129(12):745-751(2008)Ben-Shachar, D., et al. PLoS ONE 2 (9), E817 (2007) :
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