Prealbumin is composed of four identical subunits, each contributing to its stability and function. The protein’s primary role is to bind and transport thyroxine and retinol-binding protein (RBP) complexed with retinol. This binding is essential for the proper distribution of these molecules, which are vital for various physiological processes, including metabolism and vision .
Prealbumin is a significant marker for nutritional status due to its short half-life of approximately two days. This rapid turnover makes it a sensitive indicator of protein-energy malnutrition and other conditions affecting nutritional status . Additionally, mutations in the TTR gene are associated with several amyloid diseases, including:
Recombinant human prealbumin is produced using various expression systems, such as Escherichia coli (E. coli) and HEK 293 cells. The recombinant protein is typically purified using conventional chromatography techniques to achieve high purity levels suitable for research applications .
Recombinant prealbumin is widely used in research to study its structure, function, and role in disease. It is also utilized in high-throughput screening assays and other biochemical applications to understand better the mechanisms underlying its transport functions and interactions with other molecules .
Recombinant prealbumin should be stored at 4°C for short-term use and at -20°C for long-term storage. It is essential to avoid freeze-thaw cycles to maintain protein integrity. The protein is typically supplied in a buffer containing phosphate-buffered saline (PBS) and glycerol to enhance stability .