Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comparative Analysis of Mouse CSF Proteins in Experimental Autoimmune Encephalomyelitis Model and Cuprizone-Induced Demyelination Model by Olink Proteomics.

Molecular neurobiology·2026
Same author

Stromal-Derived Factor-1 (SDF-1/CXCL12) and Skin Wound Healing Research at the Intersection Between Regenerative Biology and Medicine.

International journal of molecular sciences·2026
Same author

Dysregulated hyaluronan metabolism drives inflammation and angiogenesis in proliferative diabetic retinopathy.

Frontiers in immunology·2026
Same author

An Inflammation-Associated Control Mechanism of Allergy by Proteolysis of IgE.

Allergy·2025
Same author

A key role of the PGC-1α/ERR-α pathway in regulation of angiogenic factors in proliferative diabetic retinopathy.

Frontiers in endocrinology·2025
Same author

Primary HSV-2 Infection in an Immunocompromised Patient Reveals High Diversity of Drug-Resistance Mutations in the Viral DNA Polymerase.

Viruses·2025

Related Experiment Video

Updated: May 13, 2026

Detection of Protease Activity by Fluorescent Peptide Zymography
09:56

Detection of Protease Activity by Fluorescent Peptide Zymography

Published on: January 20, 2019

Zymography methods for visualizing hydrolytic enzymes.

Jennifer Vandooren1, Nathalie Geurts, Erik Martens

  • 1Laboratory of Immunobiology, Rega Institute for Medical Research, University of Leuven, KU Leuven, Belgium.

Nature Methods
|February 28, 2013
PubMed
Summary
This summary is machine-generated.

Zymography is a powerful technique for studying enzyme activity by observing substrate degradation. This review compares zymography methods, highlighting their strengths, weaknesses, and interpretations for enzyme localization and activity studies.

More Related Videos

One-step Extraction and Zymographic Analysis of Bacterial Gelatinases
07:20

One-step Extraction and Zymographic Analysis of Bacterial Gelatinases

Published on: August 1, 2025

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials
10:50

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials

Published on: April 10, 2016

Related Experiment Videos

Last Updated: May 13, 2026

Detection of Protease Activity by Fluorescent Peptide Zymography
09:56

Detection of Protease Activity by Fluorescent Peptide Zymography

Published on: January 20, 2019

One-step Extraction and Zymographic Analysis of Bacterial Gelatinases
07:20

One-step Extraction and Zymographic Analysis of Bacterial Gelatinases

Published on: August 1, 2025

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials
10:50

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials

Published on: April 10, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Zymography is a key technique for analyzing hydrolytic enzymes based on substrate degradation.
  • It provides insights into enzyme activity, forms, and localization but is often misinterpreted.
  • Understanding zymography's nuances is crucial for accurate biochemical analysis.

Purpose of the Study:

  • To provide a comprehensive review and comparison of various zymography techniques.
  • To clarify the advantages, limitations, and proper interpretations of zymography data.
  • To discuss the future potential of zymography in degradomics research.

Main Methods:

  • Comparison of in-gel zymography for visualizing enzyme forms by molecular weight.
  • Discussion of in-situ zymography for localizing proteolytic activity in tissue sections.
  • Overview of in-vivo zymography for pinpointing proteolytic activity within intact organisms.

Main Results:

  • Zymography techniques offer distinct advantages for enzyme analysis.
  • Each method (in-gel, in-situ, in-vivo) has specific limitations and interpretation guidelines.
  • The review details how different zymography approaches visualize and localize enzyme activities.

Conclusions:

  • Zymography is a versatile tool for studying hydrolytic and proteolytic enzymes.
  • Accurate interpretation of zymography results is essential for reliable scientific conclusions.
  • Advancements in substrate probes and detection methods will enhance zymography's utility in degradomics.