ATF Bovine

Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains. These domains are globular moieties of about 330 amino acids each, divided into two sub-domains where the iron- and anion-binding sites are located. The binding cleft opens with iron release and closes with iron binding .

Ferric iron couples to transferrin only in the presence of an anion, usually carbonate, which serves as a bridging ligand between the metal and protein, excluding water from the coordination sites. Without the anion cofactor, iron binding to transferrin is negligible. In the presence of anions, ferric transferrin is resistant to all but the most potent chelators .

Apo Transferrin is essential for preventing iron accumulation in tissues, especially in conditions like non-transfusion dependent β-thalassemia . It is also a critical component in the cultivation of mammalian cells in vitro, acting as a transport factor for defined culture media. This property is crucial for long-term mammalian cell growth in vitro since Apo Transferrin operates in media by binding to contaminating metal ions .

Apo Transferrin bovine has been used in various applications, including:

• Basal medium for culturing bovine mammary epithelial cells
• Minimum essential medium α (MEM-α) for spermatogonial stem cells (SSCs) culture
• Induction medium for mesenchymal stem cell culture

Iron is taken into cells by receptor-mediated endocytosis of monoferric and diferric transferrin. Receptors on the outer face of the plasma membrane bind iron-loaded transferrin with high affinity. The C-terminal domain of transferrin mediates receptor binding, with diferric transferrin binding with higher affinity than monoferric transferrin or apotransferrin .

The normal half-life of iron in the circulation is about 75 minutes, and at least 80% of the iron bound to circulating transferrin is delivered to the bone marrow and incorporated into newly formed erythrocytes. Other major sites of iron delivery include the liver and spleen .