Badrilla Ltd. is a biotechnology company founded in 2003 and located in Leeds, UK. Badrilla makes and distributes exceptional monoclonal and polyclonal antibodies to cardiovascular protein and phospho-protein targets. We source excellent antibodies from academic leaders and re-validate antibodies not made by ourselves in assays of relevance to our customers. Working with outstanding academic collaborators, we are developing new technologies to calibrate immunoassays, which will enable the performance of genuinely Quantitative Western blotting, Quantitative biomarker measurement, and Quantitative diagnostics. Our aim is to provide products that work first time in the applications you deploy, which accelerate the progress of your research, and which satisfy your expectations in every way.
- Badrilla anti-phospho-phospholamban (Ser16/Thr17) antibody (1:3000) was used to perform immunoblot in order to study the Akt activity and phospholamban phosphorylation increased by adenylyl cyclase type VI.
- Badrilla Phospho-ryanodine receptor antibody was used to perform western blot in order to study the role of phosphorylation of the cAMP-dependent protein kinase regulatory subunit in modulation of PKA-AKAP interaction and calcium signaling.
- Badrilla Phospho-phospholamban antibody was used to perform western blot in order to study the role of phosphorylation of the cAMP-dependent protein kinase regulatory subunit in modulation of PKA-AKAP interaction and calcium signaling.
- Badrilla anti-phospho-PLB (Thr17) antibody was used for western blot in order to investigate the role of CaMKII in the regulation of pressure overload-induced cardiac hypertrophy to heart failure in mice.
- Badrilla phospho-Ser16-phospholamban antibody was used in western blot in order to study the role of PP2A in limiting PKA phosphorylation of phospholamban and TnI for myocyte contraction responses under beta1AR stimulation
- Badrilla anti-Ser-2808 (dPO3) antibody that specifically recognizes RyR2 unphosphorylated at Ser-2808 was used in western blot to detect the phosphorylation of RyR2 at Ser-2808.