|Other Accession||Q007T0, Q9CQA3, Q3T189, NP_002991.2|
|Other Names||Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Iron-sulfur subunit of complex II, Ip, SDHB, SDH, SDH1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 220-234 of HUMAN SDHB|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|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.|
|Function||Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).|
|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.
Complex II of the respiratory chain, which is specifically involved in the oxidation of succinate, carries electrons from FADH to CoQ. The complex is composed of four nuclear-encoded subunits and is localized in the mitochondrial inner membrane. The iron-sulfur subunit is highly conserved and contains three cysteine-rich clusters which may comprise the iron-sulfur centers of the enzyme. Sporadic and familial mutations in this gene result in paragangliomas and pheochromocytoma, and support a link between mitochondrial dysfunction and tumorigenesis.
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Cerecer-Gil, N.Y., et al. Clin. Cancer Res. 16(16):4148-4154(2010)
Schimke, R.N., et al. Am. J. Med. Genet. A 152A (6), 1531-1535 (2010) :
Hes, F.J., et al. BMC Med. Genet. 11, 92 (2010) :
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