Protein tagging is of great
importance in molecular biology research and experiments (Chase and Kuo,
2010). In research, two
protein tags, specifically Histidine (His-tag) and Green Fluorescent Protein
(GFP), are used to study the function, cellular pathways, and interactions
between proteins (Murayama
and Kobayashi 2014). As protein tagging is employed
more frequently, the knowledge on molecular and cellular biology concepts
continue to expand.

His-tags or polyhistidine tags are amino acid
chains comprising of approximately six histidine residues incorporated into the
N or C terminus of a target protein (Chase and Kuo, 2010). The His-tag is expressed
in a vector, and fused in the frame of the protein of interest to facilitate
protein purification (Chase and Kuo, 2010). Protein purification allows for the
removal of weakly bound contaminants from the recombinant protein to study its structure
and function (Ghahremanzadeh et al.,
2017). Understanding of the composition and physiology aids to determine therapeutic
applications for a target protein (Ghahremanzadeh et al.,
2017). Purifying a protein can be done via immobilized metal affinity
chromatography (IMAC) (Chase and Kuo, 2010). IMAC is a technique that exploits
histidine residues by separating them from His-tagged proteins (Ghahremanzadeh et al., 2017). Histidine
residues have a high affinity for metal ions such as Cu2+, Co2+,
Zn2+, and Ni2+ (Barbosa et al.,

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