Journal
/
Biochimie
/
Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
Journal JoVE
Biochimie
Un abonnement à JoVE est nécessaire pour voir ce contenu.  Connectez-vous ou commencez votre essai gratuit.
Journal JoVE Biochimie
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

•

07:32 min

•

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

Automatically generated

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.

Explore More Videos

Bacterial ExpressionRecombinant MMP-3Affinity ChromatographyE. ColiR2DP Cell StrainMMP InhibitorsProtein PurificationProtein FoldingPost-translational ProcessingIPTG InductionCell LysisInclusion Body SolubilizationSonicationCentrifugation

Read Article

Cite this Article

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).

Download .ris file

Copy

Share Video

.

Copy