Ferritin Human

Ferritin is a ubiquitous protein found in both prokaryotes and eukaryotes, playing a crucial role in iron storage and homeostasis. It serves as the primary intracellular depot for iron, sequestering it in a soluble and non-toxic form for controlled release. This iron-containing protein complex is predominantly found in the intestinal mucosa, spleen, and liver. Ferritin's structure consists of 24 subunits of heavy and light chains, with variations in subunit composition potentially influencing iron uptake and release rates in different tissues. Notably, defects in the light chain ferritin gene have been linked to neurodegenerative diseases and hyperferritinemia-cataract syndrome. The genes encoding these chains are located on different chromosomes: light chain genes on chromosome region 19q13.3-q13.4 and heavy chain genes on 11q12-q13. Structurally, ferritin resembles a hollow sphere, storing iron in its ferric (Fe(III)) oxidation state within a mineral ferrihydrite core ([FeO(OH)]8[FeO(H2PO4)]) attached to its inner wall. Iron release, essential for various physiological processes, requires its reduction to the ferrous (Fe(II)) state, allowing it to exit through channels in the sphere. This intricate structure underscores ferritin's vital role in the controlled storage and release of iron, crucial for maintaining iron homeostasis.

Human Ferritin, a glycoprotein synthesized in the liver, exhibits a molecular mass of 440-450 kDa and an isoelectric point (pI) of 5.5. This protein plays a critical role in iron storage, sequestering iron atoms in their ferric state within cells. As the primary intracellular iron store, ferritin levels in serum directly correlate with total body iron stores, making it a valuable marker for assessing iron status in conditions like anemia. Beyond iron homeostasis, ferritin serves as a marker for inflammation and holds potential in monitoring and predicting future cardiovascular events in coronary artery disease.

A clear, brownish solution that has been sterilized by filtration.

The ferritin protein is provided in a solution containing 0.05M TRIS buffer at pH 7.5, along with 1.0M NaCl and 0.09% NaN3 as preservatives.

To maintain stability, Human Ferritin should be stored refrigerated at a temperature of 2-8 degrees Celsius.

The purity of this Human Ferritin product is greater than 96.0%, ensuring high quality for research and applications.

The tissue sample used in the production of this Human Ferritin has undergone rigorous testing and been found negative for HIV-1 and HIV-2 antibodies, Hepatitis B surface antigen, Syphilis RPR, and Hepatitis C antibodies, ensuring safety and compliance with industry standards.

Human Liver.