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NDUFV1 Antibody(N-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession P49821
Clone Names 100623327
Additional Information
Gene ID 4723
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.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name NDUFV1 (HGNC:7716)
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}
Research Areas
Citations (0)
citation

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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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$ 277.78
Cat# BP19414a
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