Mentor
Zeina Alraawi
Keywords
Protein purification, Protein Tag, Angiogenesis, Anginex
Abstract
Anginex is a cytokine-like β-sheet forming peptide of 33 amino acids with potent anti-angiogenic activity.Anginex is essential in inhibiting abnormal processes caused by angiogenesis, such as tumor growth and blood vessel formation. However, Anginex has limitations, including poor stability, short half-life, complicated synthesis, and low purity. Rubredoxin dimer (RdRd) is used as a protein tag to improve stability and detection of Anginex during purification for the first time. A plasmid was designed to contain the RdRd-Anginex fusion protein. RdRd-Anginex plasmid was transformed and expressed in E. coli BL21star cells. The results show RdRd-Anginex has been purified using a Nickel Sepharose column. Enterokinase, a proteolytic enzyme, was then used to cleave between the RdRd from Anginex. The cleaved sample was placed on a Nickel Sepharose column where the Anginex sample was eluted.
Recommended Citation
Kolluru, S. (2023). Purification of Anginex: An Inhibitor of Tumor Metastasis using RdRd tag. Inquiry: The University of Arkansas Undergraduate Research Journal, 22(2). Retrieved from https://scholarworks.uark.edu/inquiry/vol22/iss2/5
