Greater than 85.0% as determined by SDS-PAGE.
Angiogenin is a 14-kilodalton ribonuclease enzyme that plays a crucial role in various physiological and pathological processes. It is involved in tumorigenesis, neuroprotection, inflammation, innate immunity, reproduction, tissue regeneration, and cellular stress responses . Human recombinant angiogenin is a synthetically produced version of this enzyme, designed to mimic its natural counterpart.
Angiogenin was first discovered in 1985 by Bert L. Vallee and his colleagues. It is a member of the ribonuclease A superfamily and shares structural similarities with other ribonucleases. The enzyme consists of 123 amino acids and has a molecular weight of approximately 14 kDa . Its three-dimensional structure includes a characteristic ribonuclease fold, which is essential for its enzymatic activity.
Angiogenin is known for its ability to induce angiogenesis, the process of forming new blood vessels from pre-existing ones. This function is critical for wound healing, tissue regeneration, and the growth of tumors. Angiogenin achieves this by binding to specific receptors on endothelial cells, stimulating their proliferation and migration .
In addition to its role in angiogenesis, angiogenin has several other biological functions:
Human recombinant angiogenin is produced using recombinant DNA technology, typically in Escherichia coli (E. coli) expression systems. The recombinant protein is purified to high levels of purity, often exceeding 97% . It retains the biological activities of the natural enzyme, including its ribonucleolytic activity and ability to induce angiogenesis .
Recombinant angiogenin has several potential clinical and research applications: