85-1404-05　Stearoyl CoA Desaturase 3, Control Peptide Mouse (SCD3) 100ug　S7900-10

特徴

• 13aa peptide of Mouse SCD-3 .
• Stearoyl-CoA desaturase (SCD, also known as Delta-9 desaturase) is an iron containing membrane enzyme. It catalyzes the rate limiting step in the biosynthesis of mono-unsaturated fatty acids. The enzyme inserts a cis double bond between the C9 and the C10 positions in the acyl-CoA derivatives of saturated fatty acids such as palmitic acid and stearic acids to produce palmitoleoyl- and oleoyl-CoA, respectively. Mono-unsaturated fatty acids play an important role in many processes, including energy metabolism (triacylglycerol storage in adipose tissues), anti-oxidation, lipid acivated signal transduction, apoptosis, mitogenesis in certain tumors, and activate certain hormone receptors. SCD genes are tightly regulated by signals such as insulin, leptin, carbohydrate, fatty acids and temperature. Three SCD genes SCD1, SCD2 and SCD3 have been identified in mouse. All three genes have been mapped at mouse chromosome 19 D2. However, in human only one structural SCD-gene (chromosome 10) encoding two SCD transcripts has been identified. The SCD-gene products (SCD-1, 2 and 3) are integral membrane proteins with four TM domains containing a novel sterol regulatory element binding protein (SREBP) binding site. SREBP regulates enzymes involved in cholesterol, triglyceride and fatty acid metabolism. The SCD enzymes have a 30aa N-terminal seq responsible for their rapid degradation and short half life of 3-4 hours.
• SCD-3: Is an integral membrane protein (mouse 359aa) with four TM domains. SCD-3 expression is limited to the differentiated sebaceous glands in mouse skin. The mouse SCD-3 protein is ~89 and 85% identical to SCD-1 and SCD-2, respectively. The enzyme is more abundant (four fold higher) in male than female. The novel sterol regulatory element binding protein (SREBP) and NF-Y binding sites, present in SCD-1 and -2, is not non-functional in SCD-3.