Human SCD‑1 Alexa Fluor™ Plus 488‑conjugated Antibody

SCD-1 (Stearoyl-CoA desaturase 1; also Acyl-CoA desaturase, fatty acid desaturase, and Delta-9 desaturase) is a 37-40 kDa member of the fatty acid desaturase family of enzymes. It is an ER-embedded protein that is expressed by multiple cell types, including adipocytes, hepatocytes, macrophages, endothelial and sebaceous gland cells. SCD-1 catalyzes the formation of monounsaturated fatty acids from saturated fatty acids. It does so by generating a double bond between the C9 and C10 carbons of dietary and/or endogenously synthesized fatty acids. This creates either palmitoleic or oleic acid, two fatty acids that are optimally suited for either storage or inclusion into phospholipids. It also removes a potential source of inflammation, as saturated fatty acids are known to activate TLRs with the subsequent onset of inflammation. Human SCD-1 is a 4-transmembrane (TM), 359 amino acid (aa) protein. It contains a 71 aa cytoplasmic N-terminus, followed by two TM segments (aa 72-119) and an extended cytoplasmic region (aa 120-216) that possesses three utilized Ser/Thr phosphorylation sites, two additional TM segments (aa 217-273), and a C-terminal cytoplasmic tail (aa 274-359) that contains most of the catalytic region. There is one potential isoform variant that shows a 13 aa substitution for aa 295-359. Over aa 141-221, human SCD-1 shares 95% aa sequence identity with mouse SCD-1.