Figure 1.
![(a) Chemical structure of S5A1. (b) S5A1 is a high-affinity ligand of SSTR5. Binding of [3H]-S5A1 to membranes expressing human SSTR5 was quantified using an SPA. [3H]-S5A1 binding to membranes was measured in the absence (total) or presence of an unlabeled competitor to determine nonspecific binding. S5A1 bound with a Kd of 260 pM, specific binding was >90%, and the maximum number if binding sites was 25 pmol/mg of protein. Data plotted are a representative experiment from three that were conducted.](https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/endo/158/11/10.1210_en.2017-00639/1/en.2017-00639f1.jpeg?Expires=1750849429&Signature=kzWrVmEZINfvjQu46jfaGNuKYh2fKmNrZvCXsnOzodJpFqABOMH4AjBiWFwIEwY5gCzfETIOtCcaCte9u0ATrnJ2LSYvD9OugmZSdH74cKtDNjZPBQx~98eaiYMZ~vcwvGn7bgxAN7UgYvklS4lJWrumtextqEjvkeZvLSVlm-cjqsr5sOAWlIZBMdYYJVKn4D8hJ6xarisU2sPv6kkie2EMnqzjJq9esVgHYtrfmqxSBvDqzchMmRiTZ7inoOgp14vT4o4ecVJgpAd9qzfE-bMRmPp41QGyR8tIi0SlTVhezTyCH0UsjlXpJifR06~yrRfA9bVeXk9Yc4rH6L3qAg__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
(a) Chemical structure of S5A1. (b) S5A1 is a high-affinity ligand of SSTR5. Binding of [3H]-S5A1 to membranes expressing human SSTR5 was quantified using an SPA. [3H]-S5A1 binding to membranes was measured in the absence (total) or presence of an unlabeled competitor to determine nonspecific binding. S5A1 bound with a Kd of 260 pM, specific binding was >90%, and the maximum number if binding sites was 25 pmol/mg of protein. Data plotted are a representative experiment from three that were conducted.
