Kinase experiment:

[3H]LY2119620 equilibrium binding is achieved by incubating 15 μg membranes, orthosteric ligand (100 μM), and various concentrations of [3H]LY2119620 (0.2 to 60 nM) for 1 hour at 25℃. The specific binding versus time data are fit to a one-site specific binding model, and the Bmax and Kd for the allosteric molecule are calculated for each orthosteric ligand[1].

LY2119620 is a selective positive allosteric modulator of M2/M4 receptor [1].

Muscarinic acetylcholine receptors (M1-M5) are G-protein coupled receptors regulating the action of the neurotransmitter ACh and play an important role in smooth muscle control, exocrine gland function, mood and cognition [1].

LY2119620 is a selective positive allosteric modulator of M2/M4 receptor. In [35S]GTPγS-binding experiments, LY2119620 exhibited a modest allosteric agonism of 23.2% and 16.8% at the M2 and M4 receptors, respectively. LY2119620 and ACh binding caused cooperativity factor α of 79.4 and 19.5 for the M4 receptor and the M2 receptor, respectively. The cooperativity between LY2119620 and orthosteric agonists (Iperoxo or Oxo-M) was also observed [1]. M2 receptor simultaneously bound to LY2119620 and iperoxo. LY2119620 exhibited mild negative cooperativity with the inverse agonist NMS and strong positive cooperativity with iperoxo [2]. LY2119620 significantly increased Bmax values without changes in Kd when cooperativity binding of [3H]LY2119620 with mAChR, suggesting a G protein-dependent process [3].

References:
[1].  Croy CH, Schober DA, Xiao H, et al. Characterization of the novel positive allosteric modulator, LY2119620, at the muscarinic M(2) and M(4) receptors. Mol Pharmacol, 2014, 86(1): 106-115.
Kruse AC, Ring AM, Manglik A, et al.  Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature, 2013, 504(7478): 101-106.
Schober DA, Croy CH, Xiao H, et al.  Development of a radioligand, [(3)H]LY2119620, to probe the human M(2) and M(4) muscarinic receptor allosteric binding sites. Mol Pharmacol, 2014, 86(1): 116-123.