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Related Concept Videos

Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

19.1K
In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or...
19.1K

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Related Experiment Video

Updated: Apr 14, 2026

Measurement of Cyclic Guanosine Monophosphate (cGMP) in Solid Tissues using Competitive Enzyme-Linked Immunosorbent Assay (ELISA)
07:15

Measurement of Cyclic Guanosine Monophosphate (cGMP) in Solid Tissues using Competitive Enzyme-Linked Immunosorbent Assay (ELISA)

Published on: July 3, 2025

858

ELISA-Based Enzyme Kinetics Assay for Measuring cGAS Activity.

Cécile Fréreux1, Philip H Howe1

  • 1Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.

Bio-Protocol
|April 13, 2026
PubMed
Summary
This summary is machine-generated.

A new ELISA method quantifies cyclic GMP-AMP synthase (cGAS) activity by measuring 2'3'-cGAMP production. This accessible assay provides reliable enzyme kinetics without specialized equipment.

Keywords:
2′3′-cGAMP synthesisAccessibleELISAEnzyme kineticsMichaelis–MentenVmaxcGASk1/2kcat

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Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Cyclic GMP-AMP synthase (cGAS) is a crucial cytosolic DNA sensor initiating innate immune responses.
  • cGAS synthesizes 2'3'-cGAMP, a second messenger activating downstream signaling pathways with potential antitumor effects.
  • Accurate measurement of cGAS enzymatic activity is vital for mechanistic and therapeutic studies.

Purpose of the Study:

  • To develop a rapid and accessible ELISA-based protocol for quantifying 2'3'-cGAMP product formation.
  • To enable derivation of cGAS enzymatic parameters using standard laboratory equipment.
  • To offer a sensitive alternative to traditional, equipment-intensive kinetic assays.

Main Methods:

  • Utilized a commercially available 2'3'-cGAMP ELISA kit for product quantification.
  • Initiated cGAS reactions with defined DNA ligands and quenched at multiple time points.
  • Calculated initial velocities from time course measurements to determine Michaelis-Menten parameters.

Main Results:

  • Established an ELISA protocol for direct, product-specific quantification of 2'3'-cGAMP.
  • Enabled determination of cGAS kinetic parameters including V0, Vmax, kcat, and k1/2.
  • Achieved reproducible kinetic results within approximately 4 hours.

Conclusions:

  • The developed ELISA protocol offers a sensitive and broadly applicable method for cGAS enzyme kinetics.
  • This accessible approach allows researchers without advanced instrumentation to reliably measure cGAS activity.
  • The protocol is suitable for evaluating modulators of cGAS activity and assessing kinetics with diverse substrates.