University of Arkansas, Fayetteville
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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.

Included in

Biochemistry Commons

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