Description
Description: This assay employs a two-site sandwich ELISA to quantitate FTMT in samples. An antibody specific for FTMT has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any FTMT present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for FTMT is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of FTMT bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: Mitochondrial ferritin was recently identified as a protein precursor. It is classified as a metal-binding protein which is located within the mitochondria. After the protein is taken up by the mitochondria it can be processed into a mature protein and assemble functional ferritin shells. Its structure was determined at 1.70 angstroms through the use of X-ray diffraction and contains 182 residues. It is 67% helical. The Ramachandran plot shows that the structure of mitochondrial ferritin is mainly alpha helical with a low prevalence of beta sheets.
Mitochondrial ferritin has many roles pertaining to molecular function. It participates in ferroxidase activity, binding, iron ion binding, oxidoreductase activity, ferric iron binding, metal ion binding as well as transition metal binding