PeptideDB

Rp-8-CPT-cAMPS

CAS No.: 129735-01-9

Rp-8-CPT-cAMPS is a powerful and competitive antagonist of cAMP-induced activation of cAMP-dependent protein kinase (PKA
Sales Email:peptidedb@qq.com

This product is for research use only, not for human use. We do not sell to patients.

Description Rp-8-CPT-cAMPS is a powerful and competitive antagonist of cAMP-induced activation of cAMP-dependent protein kinase (PKA) I and II. Acting as a potent cAMP analog, Rp-8-CPT-cAMPS exhibits a preference for site A of RI over site A of RII. Additionally, it favors site B of RII over site B of RI. This compound effectively inhibits cAMP-dependent PKA activation and demonstrates selectivity in binding to specific sites within the protein kinase.
In vitro Rp-8-CPT-cAMPS (100 μM; 15 min) blocks phosphorylation of VASP by 6-Bnz-cAMP and largely reduces VASP phosphorylation by forskolin and fenoterol[2]. Rp-8-CPT-cAMPS (100 μM; 30 min) reduces GTP-loading of Rap1 by both 8-pCPT-2'-O-Me-cAMP and 6-Bnz-cAMP[2]. Rp-8-CPT-cAMPS (100 μM; 30 min) largely diminishes the augmentation of bradykinin-induced IL-8 release by the PKA activator 6-Bnz-cAMP and the Epac activator 8-pCPT-2'-O-Me-cAMP[2]. Rp-8-CPT-cAMPS (10 μM) inhibits the endothelium-dependent and -independent relaxation which induced by Venom in pre-contracted rat mesenteric artery rings[3].
molecular weight 487.87
Molecular formula C16H15ClN5O5PS2
CAS 129735-01-9
Storage Powder: -20°C for 3 years | In solvent: -80°C for 1 year
References 1. Dostmann WR , et, al. Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3',5'-cyclic phosphorothioates. J Biol Chem. 1990 Jun 25;265(18):10484-91. 2. Roscioni SS, et, al. PKA and Epac cooperate to augment bradykinin-induced interleukin-8 release from human airway smooth muscle cells. Respir Res. 2009 Sep 29;10(1):88. 3. Chaisakul J, et, al. In vivo and in vitro cardiovascular effects of Papuan taipan (Oxyuranus scutellatus) venom: Exploring sudden collapse". Toxicol Lett. 2012 Sep 3;213(2):243-8."