Question:

Which purification method is commonly used when recombinant proteins carry a His-tag?

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His-tagged proteins are commonly purified using \[ \boxed{\text{Immobilized Metal Affinity Chromatography (IMAC)}} \] where the tag binds to \[ \boxed{\mathrm{Ni^{2+}} \text{ or } \mathrm{Co^{2+}}.} \]
Updated On: Jul 14, 2026
  • Ion exchange chromatography
  • Gel filtration chromatography
  • Affinity chromatography
  • Ultracentrifugation
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The Correct Option is C

Solution and Explanation

Step 1: Recall the purpose of a His-tag. A His-tag consists of several histidine residues attached to a recombinant protein to facilitate its purification.

Step 2:
Identify the purification method. Histidine residues bind specifically to immobilized metal ions such as \[ \boxed{\mathrm{Ni^{2+}} \text{ or } \mathrm{Co^{2+}}.} \] This property is exploited in \[ \boxed{\text{Affinity chromatography}} \] to selectively purify the recombinant protein. Therefore, \[ \boxed{(C)} \] is the correct answer.
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