Alexa Fluor® 647 Anti-Ryanodine Receptor antibody [EPR21796]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The ryanodine receptor also known as RyR is a significant calcium ion channel that facilitates the release of calcium from the sarcoplasmic reticulum into the cytosol. It is especially important in cardiac and skeletal muscle cells influencing muscle contraction. The receptor exists in three isoforms: RyR1 RyR2 and RyR3 with RyR1 dominant in skeletal muscle RyR2 in cardiac muscle and RyR3 more ubiquitously in the body. RyR is a large protein with a mass of approximately 2 megadaltons comprising multiple subunits and forming part of a transmembrane complex.

Biological function summary

These receptors regulate calcium ions important for triggering muscle contractions and other calcium-dependent processes. RyR operates as part of a complex with other proteins such as FKBP12 (calstabin) and calmodulin which modulate its function. The receptor plays an important role in excitation-contraction coupling in muscles ensuring proper physiological responses to stimuli. Calcium release through these channels not only manages contraction but also assists in signal transduction within various cellular contexts.

Pathways

The ryanodine receptor integrates significantly into the excitation-contraction coupling and the calcium signaling pathways. In excitation-contraction coupling the receptor responds to electrical stimuli by releasing calcium that initiates contraction. In the calcium signaling pathway it participates by releasing and regulating intracellular calcium level interacting with proteins such as L-type calcium channels and calsequestrin to maintain cell homeostasis. These interactions define the RyR's role in cellular respiration muscle contraction and other physiological processes.

Associated diseases and disorders

Abnormal function or mutations in RyR often associate with cardiac and skeletal muscle diseases such as malignant hyperthermia and catecholaminergic polymorphic ventricular tachycardia. Dysregulation or mutation-induced alterations affect calcium release and contribute to pathogenesis. Connections between RyR dysfunction and other proteins such as junctin or triadin in muscle cells frequently disrupt normal muscle function illustrating RyR's significant role in these disorders. The receptor's involvement in calcium dysregulation suggests potential avenues for therapeutic interventions.