Synthetic Covalently Linked Dimeric Form of H2 Relaxin Retains Native RXFP1 Activity and Has Improved In Vitro Serum Stability

Figure 4

Binding and activity of synthetic H2 (PEG)₇ H2 dimer in comparison to native H2. (a) Competition binding of H2 (PEG)₇ H2 dimer with europium-labeled H2 relaxin in HEK-293T cells stably expressing RXFP1. (b) cAMP activity in RXFP1 expressing HEK-293T cells using a pCRE-β-galactosidase reporter gene system. Data are expressed as percentage of cAMP response and are pooled data from at least three independent experiments performed in triplicate.

(a) RXFP1 Eu-H2 binding

(b) RXFP1 cAMP activity