EC Number   |
Application |
Reference |
|---|
   1.13.12.24 | analysis |
a fusion protein composed of the synthetic IgG-binding domain (ZZ domain) derived from Staphylococcus aureus protein A and apoaequorin (apoAQ) is expressed in Escherichia coli periplasm. Incubation with coelenterazine gives ZZ-aequorin which can be used as a reporter for detecting IgG. The measurable range of IgG coated on a 96-well plate is 1-1000 ng/ml |
746377 |
| 1.13.12.24 | analysis |
fusion of aequorin to orange and various red fluorescent proteins to identify the best acceptor in red emission bands. Tandem-dimer tomato-aequorin shows the highest BRET efficiency (largest energy transfer critical distance R0) and percentage of counts in the red band of all the fusions studied. Light output is sufficient to image ATP-induced Ca2+ oscillations in single HeLa cells expressing tandem-dimer tomato-aequorin. Ca2+ rises caused by depolarization of mouse neuronal cells in primary culture are also recorded, and changes in fine neuronal projections are spatially resolved. It is possible to visualize the Ca2+ activity of HeLa cells injected subcutaneously into mice, and Ca2+ signals after depositing recombinant tandem-dimer tomato-aequorin in muscle or the peritoneal cavity |
746238 |
| 1.13.12.24 | analysis |
in presence of O2 and coelenterazine, apoaequorin forms an aequorin 2-hydroperoxide. When pretreated with dithiothreitol, photoirradiation of the aequorin 2-hydroperoxide leads to formation of the dithiothreitol-modified cysteine residues located near the chromophore to sulfinic acid or sulfenic acid |
744479 |
| 1.13.12.24 | analysis |
mutant D119A is suitable for measuring Ca2+ inside the endoplasmic reticulum, the mitochondria, endosomes and the outside of live cells |
744205 |
| 1.13.12.24 | analysis |
use of the enzyme as an instrument to monitor the development of high specific DNA aptamers |
765520 |
| 1.13.12.24 | synthesis |
expression in Saccharomyces cerevisiae. The cells accumulate sufficient amounts of recombinant apoaequorin. The protein is active and not toxic to the cells |
744204 |
| 1.13.12.24 | synthesis |
overexpression of apoaequorin in Escherichia coli, solubilization of inclusion bodies with urea, purification and refolding of His6-apoaequorin in a single chromatographic step by immobilized metal-ion affinity chromatography using Ni2+-nitrilotriacetic acid agarose.The purity is greater than 80%, the yield is 0.71mg apoaequorin from a 50 ml bacterial culture. The luminescence of the purified aequorin is a linear function of its concentration extending over six orders of magnitude |
746382 |
