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Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
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Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography

4,119 Views

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07:32 min

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March 30, 2022

DOI:

10.3791/63263-v

DOI:
10.3791/63263-v

•

07:32 min
March 30, 2022

•

8 Views
, ,
1Department of Chemical & Materials Engineering,University of Nevada, Reno

Summary

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His-tag purification, dialysis, and activation are employed to increase yields of soluble, active matrix metalloproteinase-3 catalytic domain protein expression in bacteria. Protein fractions are analyzed via SDS-PAGE gels.

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Bolt, A. J., Do, L. D., Raeeszadeh-Sarmazdeh, M. Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography. J. Vis. Exp. (181), e63263, doi:10.3791/63263 (2022).

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