|Other Names||Cysteine desulfurase, mitochondrial, NFS1, NIFS|
|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||Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor.|
|Cellular Location||Isoform Mitochondrial: Mitochondrion.|
|Tissue Location||Predominantly expressed in heart and skeletal muscle. Also found in brain, liver and pancreas|
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Provided below are standard protocols that you may find useful for product applications.
Iron-sulfur clusters are required for the function of manycellular enzymes. The proteins encoded by this gene supplyinorganic sulfur to these clusters by removing the sulfur fromcysteine, creating alanine in the process. This gene uses alternatein-frame translation initiation sites to generate mitochondrialforms and cytoplasmic/nuclear forms. Selection of the alternativeinitiation sites is determined by the cytosolic pH. The encodedproteins belong to the class-V family of pyridoxalphosphate-dependent aminotransferases. Alternatively splicedtranscript variants have been described.
Naamati, A., et al. J. Biol. Chem. 284(44):30200-30208(2009)Marelja, Z., et al. J. Biol. Chem. 283(37):25178-25185(2008)Wu, C., et al. Proteomics 7(11):1775-1785(2007)Lamesch, P., et al. Genomics 89(3):307-315(2007)Biederbick, A., et al. Mol. Cell. Biol. 26(15):5675-5687(2006)
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