Several proteins mediate the biosynthesis of cholesterol. The first specific step in the cholesterol biosynthetic pathway is the conversion of transfarnesyl-diphosphate to Squalene, which is catalyzed by the endoplasmic reticulum membrane-associated enzyme Squalene synthetase, also designated Squalene synthase and Farnesyl-diphosphate farnesyltransferase. Squalene synthetase is located at a branch point in the mevalonate pathway and is also involved in isoprenoid biosynthesis. Squalene epoxidase, also designated Squalene monooxygenase, is a multi-pass microsomal membrane-associated enzyme that catalyzes the first oxygenation step in sterol biosynthesis and most likely functions as one of the rate-limiting enzymes in this pathway. Squalene epoxidase may form a complex with Squalene synthetase.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Squalene epoxidase of mouse and human origin by WB IP IF IHC(P) and ELISA
Tissue Specificity
recommended for detection of Squalene epoxidase of mouse and human origin by WB, IP, IF, IHC(P) and ELISA