Binding affinities of Ei24N and CanRch1 to IMPs
| B-GST protein | His-IMP | Kd | Bmax |
| nM | % | ||
| Ei24N | IMPβ1 WT | 5.1 ± 0.6 | 100 ± 0.06 |
| IMPβ1 IBBm | ND | 24.0 ± 5.0 (P < 0.001) | |
| IMPα2 WT | 7.3 ± 1.4 | 48.0 ± 5.8 (P < 0.001) | |
| IMPα2ΔIBB | 4.4 ± 2.2 | 101 ± 12 | |
| CanRch1 | IMPβ1 WT | 4.5 ± 0.5 | 100 ± 0.2 |
| IMPβ1 IBBm | ND | 10.0 ± 2.5 (P < 0.001) | |
| IMPα2 WT | 6.6 ± 3.5 | 48.4 ± 9.3 (P < 0.05) | |
| IMPα2ΔIBB | 9.6 ± 2.1 | 86.2 ± 7.0 |
| B-GST protein | His-IMP | Kd | Bmax |
| nM | % | ||
| Ei24N | IMPβ1 WT | 5.1 ± 0.6 | 100 ± 0.06 |
| IMPβ1 IBBm | ND | 24.0 ± 5.0 (P < 0.001) | |
| IMPα2 WT | 7.3 ± 1.4 | 48.0 ± 5.8 (P < 0.001) | |
| IMPα2ΔIBB | 4.4 ± 2.2 | 101 ± 12 | |
| CanRch1 | IMPβ1 WT | 4.5 ± 0.5 | 100 ± 0.2 |
| IMPβ1 IBBm | ND | 10.0 ± 2.5 (P < 0.001) | |
| IMPα2 WT | 6.6 ± 3.5 | 48.4 ± 9.3 (P < 0.05) | |
| IMPα2ΔIBB | 9.6 ± 2.1 | 86.2 ± 7.0 |
Pooled data (n ≥ 3) from AlphaScreen assays performed as per Fig. 3 for the binding affinities (Kd) and maximal binding (Bmax) expressed as a percentage of Bmax relative to IMPβ1 for Ei24N and CanRch1, respectively. Results are for the mean ± SEM, with significant differences in maximal binding relative to IMPβ1 denoted by p-values. Harreman et al. (2003b) showed that binding of the IMPα IBB to IMPβ1 and IMPα2ΔIBB is near identical in terms of Kd.