SCAP Antibody recognizes endogenous levels of total SCAP protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly193 of human SCAP protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
SREBP cleavage activating protein (SCAP) is a membrane-bound protein essential in regulating sterol regulatory element binding protein (SREBP) processing (1). In cholesterol-starved cells, SREBPs move from the ER to the Golgi apparatus with the help of SCAP, where the precursor SREBPs are cleaved by site-1 (S1P) and site-2 (S2P) proteases (1,2). Released SREBP amino-terminal domains enter the nucleus and bind to sterol response elements located in the promoters of a number of genes responsible for the cholesterol synthesis (1,2). Research studies show that the SCAP/SREBP pathway is critical for diabetic fatty liver development and carbohydrate-induced hypertriglyceridemia in mice (3). In addition, the SCAP/SREBP pathway is required to protect cancer cells from lipotoxicity (4).