Dystrophin (C-terminal Domain) [MANDRA1]

Dystrophin is a rod-shaped protein, measuring about 150 nm, consisting of 3684 amino acids with a calculated molecular weight of 427 kDa. Dystrophin can be separated into four domains: N-terminal actin binding domain (amino acids 14-240), central rod domain (amino acids 253-3040), Cysteine-rich domain (amino acids 3080-3360), and C-terminal domain (amino acids 3361-3685). Its N-terminal domain binds to F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. Its C-terminal domain binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. Pathogenic mutations in dystrophin result in Duchenne (DMD) and Becker (BMD) muscular dystrophies. This clone is recommended for detection of an epitope corresponding to amino acids 3558-3684 of dystrophin C-terminal domain.