|Application ||WB, E|
|Other Accession||Q91YT0, Q8HXQ9, P25708, NP_009034.2|
|Predicted||Bovine, Monkey, Mouse|
|Calculated MW||50817 Da|
|Antigen Region||21-50 aa|
|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|
|Target/Specificity||This NDUFV1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 21-50 amino acids from the N-terminal region of human NDUFV1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NDUFV1 Antibody(N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).|
|Cellular Location||Mitochondrion inner membrane; Peripheral membrane protein; Matrix side|
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Provided below are standard protocols that you may find useful for product applications.
The mitochondrial respiratory chain provides energy to cells via oxidative phosphorylation and consists of four membrane-bound electron-transporting protein complexes (I-IV) and an ATP synthase (complex V). This gene encodes a 51 kDa subunit of the NADH:ubiquinone oxidoreductase complex I; a large complex with at least 45 nuclear and mitochondrial encoded subunits that liberates electrons from NADH and channels them to ubiquinone. This subunit carries the NADH-binding site as well as flavin mononucleotide (FMN)- and Fe-S-biding sites. Defects in complex I are a common cause of mitochondrial dysfunction; a syndrome that occurs in approximately 1 in 10,000 live births. Mitochondrial complex I deficiency is linked to myopathies, encephalomyopathies, and neurodegenerative disorders such as Parkinson's disease and Leigh syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
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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