Table 6.
Name | Analyte | Permutant | Sensor Unit | λex,nm | λem, nm | Kd | RA | Reference |
---|---|---|---|---|---|---|---|---|
Upward DAG | DAG | cpGFP | PKCδ without C2 domen | NM | NM | NM | 45% (in vivo) | [202] |
Downward DAG | DAG | cpGFP | PKCδ without C2 domen | NM | NM | NM | −40% (in vivo) | [202] |
Upward DAG2 | DAG | cpGFP | PKCδ without C2 domen | NM | NM | Improved version of Upward DAG | [26] | |
Downward DAG2 | DAG | cpGFP | PKCδ without C2 domen | NM | NM | Improved version of Downward DAG | [26] | |
cADDis | cAMP | cpGFP | EPAC2 | NM | NM | 10–100 μM cAMP detection | −35% (in vivo) | [205] |
cAMPr | cAMP | cpGFP | PKA-catalytic and PKA regulatory subunit Iα (RIα) | 490 | 520 | NM | 1.5-fold | [79] |
α-FlincG | cGMP | cpEGFP | Regulatory domain PKG Iα | 480 | 510 | 35 nM | 1.55-fold | [87] |
β-FlincG | cGMP | cpEGFP | Regulatory domain PKG Iβ | 480 | 510 | 1.1 μM | 2.05-fold | [87] |
δ-FlincG | cGMP | cpEGFP | Regulatory domain PKG Iα | 410/480 | 510 | 490 nM | 3.5-fold | [87] |
FlincG2 | cGMP | cpEGFP | Regulatory domain PKG Iα | 480 | 510 | Modified version of δ-FlincG | [208] | |
FlincG3 | cGMP | cpEGFP | Regulatory domain PKG Iα | 480 | 510 | Modified version of δ-FlincG | [208] | |
Btk-cpGFP | inositol-1,3,4,5-tetrakisphosphate | cpGFP | PH domain from Btk | 396/470 | 508 | 100 nM | 1.5-fold | [67] |
R-FlincA | cAMP | cp146mApple | high-affinity cAMP-binding motif from the human PKA regulatory subunit Iα (RIα) | 571 | 590 | 0.3 μM | 860% | [209] |
The raw colors refer to the colors of fluorescent proteins used as reporter domains. Kd—dissociation constant. NM – not measured. RA—response amplitude.