SCD Protein, Human (Cell-Free, His)

SCD proteins (or stearoyl-CoA desaturases) critically catalyze the introduction of the first double bond into saturated fatty acyl-CoA substrates (such as palmitoyl-CoA and stearoyl-CoA). This process produces a mixture of 16:1 and 18:1 unsaturated fatty acids, which play a crucial role in lipid biosynthesis. SCD Protein, Human (Cell-Free, His) is the recombinant human-derived SCD protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of SCD Protein, Human (Cell-Free, His) is 359 a.a., with molecular weight of 44.3 kDa.

SCD (Stearoyl-CoA desaturase) is a vital enzyme that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the introduction of the first double bond into saturated fatty acyl-CoA substrates, such as palmitoyl-CoA and stearoyl-CoA. This process results in the production of a mixture of 16:1 and 18:1 unsaturated fatty acids, playing a crucial role in lipid biosynthesis. SCD is pivotal in regulating the expression of genes associated with lipogenesis and mitochondrial fatty acid oxidation, contributing to the biosynthesis of membrane phospholipids, cholesterol esters, and triglycerides. Moreover, SCD plays a key role in maintaining body energy homeostasis, highlighting its significance in fundamental cellular processes.

Human

E. coli Cell-free

N-10*His

O00767 (M1-G359)

6319

MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG

44.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.