cytoglobin ELISA Kits

Cytoglobin is a globin protein found in vertebrate cells and is described as a hexacoordinate hemoglobin which binds ligand differently from the pentacoordinate hemoglobins. It was discovered more than a decade ago in a proteomic screen of fibrotic liver. It is involved in oxygen transport, and may be involved in protection during oxidative stress. The gene is located on chromosome 17 in the same region as a retinal gene which is mutated in progressive rod-cone degeneration, but in the opposite orientation. It is a recently discovered member of the vertebrate globin family. An intracellular protein endowed with hexacoordinated heme-Fe atoms, in their ferrous and ferric forms, and display O2 affinities comparable with that of myoglobin. Cytoglobin is expressed in many different tissues, although at varying levels. It shares common ancestry with myoglobin, and can be traced to early vertebrate evolution.

The physiological role of cytoglobin is not completely understood. Although supplying cells with O2 is the likely function, it is also possible that it act as O2-consuming enzymes or as O2 sensors. A second role may be as NADH oxidases, which facilitate the glycolytic production of ATP under semi-anaerobic conditions. Such a function has been proposed for the hexacoordinated non-symbiotic Hbs of plants, e.g. maize. It may also function as O2 sensors, participating in a signal transduction pathway that modulates the activities of regulatory proteins in response to changes in O2 concentration. It has been shown to exhibit many respiratory roles in normal cells including oxygen storage, reactive oxygen species (ROS) scavenging, terminal oxidase activity, and antifibrotic activities. Its role in respiration has been reviewed, owing to its relationship with the globin family and also due to its upregulation in hypoxia. Recently it has been reported to have some implications in cancer.