Anti-SREBF chaperone antibodies are used for the immunodetection of the protein encoded by the SCAP gene. In humans, the canonical protein has a reported length of 1279 amino acid residues and a mass of 139.7 kDa. Its subcellular localization is in the ER, Golgi, and cytoplasmic vesicles. Alternative splicing is reported to yield 4 different isoforms for this protein. A member of the WD repeat SCAP protein family, it is known to be an escort protein required for cholesterol as well as lipid homeostasis (By similarity). Post-translational modifications have been described, including ubiquitination and glycosylation. Other names for this target antigen include SREBP cleavage-activating protein, and sterol regulatory element-binding protein cleavage-activating protein. Gene orthologs have been identified in the mouse, rat, bovine, frog, zebrafish, chimpanzee and chicken species. A number of SREBF chaperone antibodies have been mentioned in research publications and have associated citations. Western Blot is a widely used application for these antibodies. ELISA, Immunofluorescence, and Immunohistochemistry are also common applications.