Ferritin Detection Service
Ferritin is a globular protein that has the function to store iron and maintain iron homeostasis in the body. It is a biomarker of great concern that is associated with inflammation, angiogenesis, malignant tumors, and recurrence of malignant diseases. Creative BioMart Biomarker offers high quality detection service for ferritin, ensuring high detection accuracy, sensitivity and efficiency for each sample.
Introduction
Ferritin is a highly symmetrical, iron-containing globular protein that is structurally characterized with a cavity that can be used to store large amounts of iron. The ferritin family consists of three subfamilies, the typical nonheme ferritin (FTN) consisting of 24 subunits, the heme-containing bacterial ferritin (BFR) also consisting of 24 subunits, and the DNA binding protein (DPS) consisting of 12 subunits. FTN is found in bacteria, plants and animals, while BFR and DPS are only found in prokaryotes. Ferritin is capable of attracting iron ions and utilizes its ferroxidase activity and special chemical activity of the cavity to induce mineralization of iron ions. The mineral core of ferritin can hold up to 4,000 mineralized forms of iron atoms and is protected by a protein coat. Ferritin subunits are sometimes referred to as heavy ferritin (H) and light ferritin (L), respectively. H-ferritin and L-ferritin function differently, H-ferritin helps to oxidize Fe2+ to Fe3+, and L-ferritin promotes the formation of an iron core. The H-ferritin is mainly present in the heart, while the L-ferritin is mainly present in the liver. In addition, the H/L ratio changes in inflammation and some pathological conditions, therefore, it can be used as a biomarker for inflammation and angiogenesis. Ferritin is mainly found in the cytoplasmic, nucleus and mitochondria, and has the function of storing iron and maintaining iron homeostasis. Iron is an important trace element in the body and a component of many proteins in mammals. However, free Fe2+ ions can catalyze the formation of reactive hydroxyl radicals through the Fenton reaction, resulting in damage to DNA, lipids and proteins, which means that iron is potentially toxic. Ferritin just happens to solve this problem by catalyzing the highly toxic Fe2+ to less toxicity Fe3+ according to its ferroxidase activity. In disease research, ferritin levels are elevated in both malignant tumor and relapsed acute leukemia cases, so ferritin may be used as a biomarker not only for malignant tumors but also for malignant disease recurrence.
Figure 1. Ferritin structure (Knovich, et al. 2009)
Application of Ferritin Detection
- Serum and plasma ferritin levels as biomarkers to predict bone diseases, such as inflammation, angiogenesis, malignant tumors.
Our Advantages
- Guarantee high accuracy and sensitivity for ferritin detection
- Ensure high repeatability of ferritin detection
- Short turn-around time of detection service
- Competitive price in the market of detection services
- Provide multiple ferritin detection methods, including ELISA and RIA
- Accept a wide range of sample types (serum, plasma, urine, etc.)
Workflow of Ferritin Detection at Creative BioMart Biomarker
Creative BioMart Biomarker strictly controls each specific experimental step in the ferritin detection procedure to ensure accurately quantify the level of ferritin in each sample.
At Creative BioMart Biomarker, we offer ferritin detection service which includes several technical methods, you can communicate with our experts according to your research needs, and we will determine the final detection technological scheme based on the communication results. Please feel free to contact us, Creative BioMart Biomarker is here to offer you professional and thoughtful service.
References:
- Knovich, M.A.; et al. Ferritin for the clinician. Blood Reviews. 2009, 23(3): 95-104.
- Arosio, P.; et al. Ferritin, cellular iron storage and regulation. IUBMB Life. 2017, 69(6): 414-422.
- Fan, K.; et al. Human ferritin for tumor detection and therapy. Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology. 2013, 5(4): 287-298.
