|Other Names||Fatty acid desaturase 2, 11419-, Delta(6) fatty acid desaturase, D6D, Delta(6) desaturase, Delta-6 desaturase, FADS2|
|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||Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma- linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum.|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
|Tissue Location||Expressed in a wide array of tissues, highest expression is found in liver followed by brain, lung, heart, and retina. A lower level is found in breast tumor when compared with normal tissues; lowest levels were found in patients with poor prognostic index.|
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The protein encoded by this gene is a member of the fattyacid desaturase (FADS) gene family. Desaturase enzymes regulateunsaturation of fatty acids through the introduction of doublebonds between defined carbons of the fatty acyl chain. FADS familymembers are considered fusion products composed of an N-terminalcytochrome b5-like domain and a C-terminal multiplemembrane-spanning desaturase portion, both of which arecharacterized by conserved histidine motifs. This gene is clusteredwith family members FADS1 and FADS2 at 11q12-q13.1; this cluster isthought to have arisen evolutionarily from gene duplication basedon its similar exon/intron organization.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Mathias, R.A., et al. J. Lipid Res. 51(9):2766-2774(2010)Lu, Y., et al. Am. J. Clin. Nutr. 92(1):258-265(2010)Zabaneh, D., et al. PLoS ONE 5 (8), E11961 (2010) :Steer, C.D., et al. PLoS ONE 5 (7), E11570 (2010) :
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