Recombinant Proteins
Product List
Ferritin Human
Human Liver Ferritin
It can be used as a marker for inflammation and also used for monitoring and prediction of future events in coronary artery disease.
Ferritin Human, FTL
Ferritin Human Recombinant, Light Chain
FTH1 Human
Ferritin Human Recombinant, Heavy Chain
Introduction
Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. It is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals . Ferritin is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form . In humans, ferritin acts as a buffer against iron deficiency and iron overload . Ferritin can be classified based on its subunit composition into light (L) and heavy (H) chains, which are encoded by different genes .
Ferritin is a globular protein complex consisting of 24 protein subunits forming a hollow nanocage with multiple metal–protein interactions . It is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier . The expression patterns of ferritin vary, with high levels observed in the liver, spleen, and bone marrow, which are key sites for iron storage . Ferritin is also present in other cell compartments, such as the nucleus, mitochondria, and lysosomes .
Ferritin’s primary function is to store iron and release it in a controlled manner to maintain iron homeostasis . It plays a crucial role in protecting cells from oxidative damage by sequestering free iron, which can catalyze the formation of reactive oxygen species . Ferritin also participates in immune responses by sequestering iron from pathogens, thereby limiting their growth . Additionally, ferritin is involved in pathogen recognition and the modulation of immune responses .
Ferritin interacts with other molecules and cells through various mechanisms. It binds to iron ions and stores them in a bioavailable and non-toxic form . The release of iron from ferritin involves the reduction of ferric iron (Fe3+) to ferrous iron (Fe2+), which is then transported out of the ferritin nanocage . Ferritin also interacts with other proteins and cellular components, influencing downstream signaling cascades related to iron metabolism and oxidative stress responses .
The expression and activity of ferritin are tightly regulated at both the transcriptional and post-transcriptional levels . Iron regulatory proteins (IRPs) bind to iron-responsive elements (IREs) in the mRNA of ferritin, controlling its translation in response to cellular iron levels . Additionally, ferritin synthesis is regulated by oxidative stress and inflammatory signals . Post-translational modifications, such as phosphorylation, also play a role in modulating ferritin activity and stability .
Ferritin has numerous applications in biomedical research, diagnostics, and therapeutics. It is used as a biomarker for iron stores and inflammation, aiding in the diagnosis of conditions like iron-deficiency anemia and hemochromatosis . Ferritin nanoparticles are explored for drug delivery and imaging purposes due to their ability to encapsulate and transport various substances . Additionally, ferritin-based therapies are being investigated for their potential in treating iron-related disorders and certain cancers .
Throughout the life cycle, ferritin plays a vital role in maintaining iron homeostasis from development to aging . During embryonic development, ferritin ensures adequate iron supply for rapid cell growth and differentiation . In adulthood, ferritin continues to regulate iron storage and release, protecting cells from oxidative damage . In aging and disease, alterations in ferritin levels and function can contribute to conditions such as neurodegenerative diseases and anemia .
