NDUFS1 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P28331 |
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Other Accession | NP_004997.4 |
Clone Names | 90625139 |
Gene ID | 4719 |
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Other Names | NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, Complex I-75kD, CI-75kD, NDUFS1 |
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 | NDUFS1 |
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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:30879903, PubMed:31557978). Essential for catalysing the entry and efficient transfer of electrons within complex I (PubMed:31557978). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:30879903, PubMed:31557978). |
Cellular Location | Mitochondrion inner membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P15690}; Matrix side {ECO:0000250|UniProtKB:P15690} |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene belongs to the complex I75 kDa subunit family. Mammalian complex I is composed of 45different subunits. It locates at the mitochondrial inner membrane.This protein has NADH dehydrogenase activity and oxidoreductaseactivity. It transfers electrons from NADH to the respiratorychain. The immediate electron acceptor for the enzyme is believedto be ubiquinone. This protein is the largest subunit of complex Iand it is a component of the iron-sulfur (IP) fragment of theenzyme. It may form part of the active site crevice where NADH isoxidized.
References
Korsten, A., et al. Biochim. Biophys. Acta 1797(2):197-203(2010)Saito, A., et al. J. Hum. Genet. 54(6):317-323(2009)Martins-de-Souza, D., et al. BMC Psychiatry 9, 17 (2009) Wang, L., et al. Cancer Epidemiol. Biomarkers Prev. 17(12):3558-3566(2008)
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