The bronchospasmolytic and secretolytic effects of ivy leaves dry extracts can be explained by an increased β₂-adrenergic responsiveness of the bronchi. Recently, it was shown that α-hederin inhibits the internalization of β₂-adrenergic receptors (ß₂AR) under stimulating conditions. α-Hederin pretreated alveolar type II cells and human airway smooth muscle cells revealed an increased ß₂AR binding and an elevated intracellular cAMP level, respectively. In order to identify whether additional compounds also mediate an increased β₂-adrenergic responsiveness, we examined the ingredients of an ivy leaves dry extract (EA 575) protocatechuic acid, neochlorogenic acid, chlorogenic acid, cryptochlorogenic acid, rutin, kaempferol-3-O-rutinoside, 3,4-, 3,5- and 4,5-dicaffeoylquinic acid, hederacoside B, and β-hederin. Within all the tested substances, only β-hederin inhibited the internalization of GFP-tagged ß₂AR in stably transfected HEK293 cells. Using fluorescence correlation spectroscopy β-hederin (1 μM, 24 h) pretreated HASM cells showed a statistically significant increase in the ß₂AR binding from 33.0 ± 8.9% to 44.1 ± 11.5% which was distributed with 36.0 ± 9.5% for τ_bound1 and 8.1 ± 2.6% for τ_bound2, respectively (n = 8, p < 0.05). The increased binding was selectively found for the receptor–ligand complex with unrestricted lateral mobility (τ_bound1 of 0.9 ± 0.1 ms, D₁ = 9.1 ± 0.2 μm²/s, n = 8), whereas the binding of ß₂AR with hindered lateral mobility (τ_bound2 of 64.2 ± 47.6 ms, D₂ = 0.15 ± 0.02 μm²/s, n = 8) was not affected. Compared to control cells, a statistically significant increase of 17.5 ± 6.4% (n = 4, p < 0.05) and 24.2 ± 5.8% (n = 4, p < 0.001) in the cAMP formation was found for β-hederin pretreated HASM cells after stimulation with 10 μM of terbutaline and simultaneous stimulation with 10 μM terbutaline and 10 μM forskolin, respectively. Within this systematic study focusing on the influence of the ingredients of an ivy leaves dry extract on HASM cells it was possible to identify β-hederin as further component presumably responsible for the β₂-mimetic effects.