|Other Names||Acyl-CoA desaturase, Delta(9)-desaturase, Delta-9 desaturase, Fatty acid desaturase, Stearoyl-CoA desaturase, SCD|
|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||Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
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Stearoyl-CoA desaturase (SCD; EC 188.8.131.52) is aniron-containing enzyme that catalyzes a rate-limiting step in thesynthesis of unsaturated fatty acids. The principal product of SCDis oleic acid, which is formed by desaturation of stearic acid. Theratio of stearic acid to oleic acid has been implicated in theregulation of cell growth and differentiation through effects oncell membrane fluidity and signal transduction. Four SCD isoforms,Scd1 through Scd4, have been identified in mouse. In contrast, only2 SCD isoforms, SCD1 and SCD5 (MIM 608370), have been identified inhuman. SCD1 shares about 85% amino acid identity with all 4 mouseSCD isoforms, as well as with rat Scd1 and Scd2. In contrast, SCD5shares limited homology with the rodent SCDs and appears to beunique to primates (Zhang et al. (1999) [PubMed 10229681]; Wang etal., 2005 [PubMed 15907797]).
Collins, J.M., et al. J. Biol. Chem. 285(9):6044-6052(2010)Peter, A., et al. Diabetes 58(8):1757-1765(2009)Carmel, J.F., et al. J. Cell. Biochem. 106(4):608-617(2009)Zhou, Y.E., et al. Metab. Clin. Exp. 58(2):158-166(2009)
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