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Transferrin

Updated: 2026-07-15

Overview

Transferrin is a glycoprotein primarily produced in the liver, responsible for the transport of iron in the bloodstream. It ensures that iron is delivered safely to cells while minimizing the risk of iron-induced oxidative damage. Transferrin is essential for maintaining iron homeostasis and is widely used in medical and research applications. Structurally, transferrin consists of a single polypeptide chain with two iron-binding sites. Its ability to bind iron tightly but reversibly makes it a critical component in both physiological and industrial contexts. The protein is available in various forms, including human serum-derived and recombinant versions.

Physical and Chemical Properties

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Transferrin has a molecular weight of approximately 80 kDa and is highly soluble in water and physiological buffers. It exhibits a high affinity for ferric iron (Fe³⁺), with each molecule capable of binding two iron ions. The iron-binding process is pH-dependent, with iron released in acidic environments such as the endosome. The protein is stable under physiological conditions but can degrade if exposed to extreme temperatures or repeated freeze-thaw cycles. Its lyophilized form is preferred for long-term storage, while liquid solutions are used for immediate applications in cell culture and diagnostics.

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Main Applications

Transferrin is widely used in cell culture media to provide bioavailable iron for cell growth. It is especially critical in serum-free media formulations, where it replaces the iron-binding proteins found in serum. Additionally, transferrin is used in medical diagnostics to assess iron status and detect conditions like iron deficiency or overload. In research, transferrin is employed to study iron metabolism, receptor-mediated endocytosis, and diseases such as hemochromatosis. Its role in drug delivery systems is also being explored, leveraging its natural ability to target specific cells via transferrin receptors.

Safety and Storage

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Transferrin is generally non-toxic and safe to handle under standard laboratory conditions. However, proper precautions should be taken to avoid contamination and degradation. Lyophilized transferrin should be stored at -20°C in a dry environment, while liquid solutions should be aliquoted to prevent repeated freeze-thaw cycles. When working with transferrin, use personal protective equipment such as gloves and lab coats. Ensure that the protein is sourced from reputable suppliers to guarantee purity and avoid potential contaminants. Always follow the manufacturer's guidelines for reconstitution and usage.

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B2B Procurement Guide

When procuring transferrin for B2B purposes, consider factors such as purity, source (human or recombinant), and supplier reliability. Human serum-derived transferrin is commonly used, but recombinant versions offer consistency and reduced risk of contaminants. Verify the protein's iron saturation level, as this affects its performance in applications like cell culture. Prices vary based on purity and quantity, with bulk purchases often offering cost savings. Request certificates of analysis (CoA) to confirm specifications such as endotoxin levels and iron-binding capacity. Establish relationships with trusted suppliers to ensure consistent quality and availability.

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