- CITATIONS: 1
|Application ||WB, FC, IHC-P, E|
|Calculated MW||20108 Da|
|Antigen Region||131-160 aa|
|Other Names||NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ, NADH-ubiquinone oxidoreductase 18 kDa subunit, NDUFS4|
|Target/Specificity||This NDUFS4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 131-160 amino acids from the C-terminal region of human NDUFS4.|
|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||NDUFS4 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in 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.|
|Cellular Location||Mitochondrion inner membrane; Peripheral membrane protein; Matrix side|
Provided below are standard protocols that you may find useful for product applications.
NDUFS4 is an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase(Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane.
Panelli,D., et.al., Biochimie 90 (10), 1452-1460 (2008)
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