MA3-927 detects triadin from mouse, rabbit and rat tissues.
MA3-927 has been successfully used in Western blot, immunohistochemistry, immunoprecipitation and ELISA procedures. By Western blot, this antibody detects a 95 kDa protein representing triadin from rabbit skeletal muscle extracts. Immunohistochemical staining of triadin in rat skeletal muscle with MA3-927 results in striated staining consistent with sarcoplasmic reticulum localization.
The MA3-927 antigen is purified rabbit fast skeletal muscle triadin.
The junction between the transverse tubules (T-tubules) and the sarcoplasmic reticulum (SR) of skeletal muscle is called the triad. At the triad, dihydropyridine receptors (DHPR's) of the T-tubule serve as voltage sensors in excitation-contraction coupling, while ryanodine receptors (RyR's), the calcium release channels, exist in the membrane of the terminal cisternae of the SR. It is thought that during slow phase depolarization of the T-tubule, a third protein, triadin (MW 95 kDa) transmits electrochemical signals to the SR through direct interaction with both DHPR's and RyR's.
Though its exact role in this signaling process is unclear, triadin has been shown to co-localize with both DHPR and RYR at the junctional face of the terminal cisternae.
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Protein Aliases: cardiac triadin; junctional sarcoplasmic reticulum glycoprotein; TRDN; Triadin; triadin 1; triadin 32 kDa (TRISK 32); triadin 49 kDa (TRISK 49); triadin 95; TRISK
Gene Aliases: 2310045H21Rik; EG432451; TDN; TRDN