FTH1 Human
Description
Product Specs
The light chain ferritin polypeptide is the primary protein responsible for storing iron inside cells in both prokaryotes and eukaryotes. The specific makeup of ferritin subunits affects how quickly iron is absorbed and released in different tissues. A crucial role of ferritin is to store iron in a way that is both soluble and non-toxic. Defects in the gene responsible for producing this light chain ferritin have been linked to various neurodegenerative diseases and a condition called hyperferritinemia-cataract syndrome.
Ferritin ensures that iron is stored in a soluble, non-toxic form that is readily available when needed. It plays a vital role in maintaining iron balance within the body. Iron is taken into the body in its ferrous form and, after being oxidized, is stored as ferric hydroxides.
Adding a carrier protein like HSA or BSA (0.1%) is recommended for extended storage.
Avoid repeated freezing and thawing.
Product Science Overview
Ferritin is a crucial iron-storage protein found in all living organisms, playing a vital role in maintaining iron homeostasis. The human recombinant ferritin heavy chain (FTH1) is a synthetic version of the naturally occurring heavy chain of ferritin, produced through recombinant DNA technology. This article delves into the structure, function, and significance of the ferritin heavy chain, particularly the human recombinant variant.
Ferritin is composed of 24 subunits, forming a hollow spherical shell that can store up to 4500 iron atoms in a non-toxic and soluble form . These subunits are of two types: heavy (H) and light (L) chains. The heavy chain, encoded by the FTH1 gene located on chromosome 11, is responsible for the ferroxidase activity of ferritin, which catalyzes the oxidation of Fe(II) to Fe(III) .
The primary function of ferritin is to store iron in a soluble, non-toxic form and release it in a controlled manner. The heavy chain of ferritin plays a critical role in this process by oxidizing Fe(II) to Fe(III), which is then stored as ferric hydroxides inside the protein shell . This oxidation process is essential for preventing the formation of free radicals, which can cause cellular damage.
Recombinant ferritin heavy chain is produced using Escherichia coli as an expression system . This recombinant protein retains the functional properties of the natural ferritin heavy chain, making it suitable for various research and clinical applications. It is often used in studies related to iron metabolism, neurodegenerative diseases, and as a control in biochemical assays .
Mutations in the FTH1 gene can lead to disorders such as Hemochromatosis type 5, characterized by excessive iron accumulation in the body . Understanding the structure and function of the ferritin heavy chain is crucial for developing therapeutic strategies for such iron-related disorders. Additionally, defects in ferritin proteins have been associated with several neurodegenerative diseases, highlighting the importance of ferritin in maintaining neuronal health .
