In the development and evolution of our species, multiple elements are fundamental, such as the protein HSA (Human Serum Albumin). This protein is the most abundant in plasma.
Therefore, we explore a little deeper into this substance, making available to you an extensive catalog of fine chemical products like this one. At DC Fine Chemicals, we ensure the quality of every substance so that you can achieve the results you desire.
Human serum albumin and its properties
Our blood is a “living tissue,” composed of both solids and liquids. In the liquid part, known as plasma, salts, water, and proteins coexist. One of these proteins is human serum albumin, the most abundant protein in blood plasma. It is a water-soluble protein synthesized in the liver.
Human serum albumin (CAS 70024-90-7) is produced in the liver and is responsible for transporting fatty acids and hormones, among other compounds. It also maintains oncotic pressure and regulates pH. In short, it is efficient for maintaining good health and for the expansion and growth of human stem cells. Additionally, it acts as a carrier for nutrients, xenobiotics, and metabolites. Its interaction with plasma zinc facilitates its absorption into cells.
It is synthesized in liver cells as pre proalbumin. This protein contains an N-terminal residue that is hydrolyzed, giving rise to a second protein called proalbumin. This proalbumin is secreted from the rough endoplasmic reticulum of the cell. At the same time, the Golgi apparatus is responsible for transforming this proalbumin into the final albumin, which is released into the bloodstream.
The gene for human serum albumin is located on chromosome 4, and mutations in it can cause abnormal proteins. It consists of 16,061 nucleotides divided into 15 exons, symmetrically located in the three existing domains. Its molecular mass is 66.5 kDa, and its half-life is around 20 days. Structurally, it is composed of three domains, two subdomains, and two regions for binding to other specific molecules – Sudlow binding regions. As shown in the attached image, the alpha secondary structure predominates in the protein.
Its presence in the pharmaceutical industry has been highlighted due to its ability to bind to other pharmacological molecules, ensuring high levels of stability during storage, biodegradability, reproducibility, and control in release properties. Additionally, it is characterized by the absence of toxic traits and antigenicity, making it commonly used in applications for medical diagnosis.
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