Dihydropyridine receptor (DHPR) is a surface membrane protein critical for the excitation-contraction coupling of striated muscle. DHPR and the sarcoplasmic reticulum ryanodine receptor (RyR) are two key components of the intracellular junctions, where depolarization of the surface membrane is converted into the release of Ca2+ from internal stores. The alpha1-subunit of the DHPR contains a cytoplasmic loop which is thought to be involved in the interactions with RyR. Phosphorylation of the DHPR alpha1-subunit is also thought to play a role in the functional interaction of DHPR and RyR. Mutation in DHPR alpha1 results in excitation-contraction uncoupling, leading to muscular dysgenesis, a complete inactivity in developing skeletal muscles. Cells that do not express RyR also lack excitation-contraction coupling and exhibit a severalfold reduction in Ca2+ current density.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
p-RyR2 (S2808)pAb detects endogenous levels of RyR2 protein only when phosphorylated at Ser2808
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