The contractile function of the skeletal muscle is based on the energetic arrangement of an odd cell type that’s extremely big, multi-nucleated and exceptionally heterogeneous in its own protein isoform composition 61 A striking biochemical quality of contractile cells is the existence of a substantial number of rather high-molecular-mass protein species 62, that can be sometimes hard to divide for proteomic research 63 The physiological coupling of human muscle fibers to its innervating motor neuron within different motor components affects skeletal muscle mass, fiber dimensions, contractile kinetics, energy metabolism, muscle cell specificity and fiber type-related protein expression routine 64 Apart from a combination of fast-twitching, slow-twitching and hybrid elements 65, person skeletal muscles also comprise several layers of connective tissue, capillaries and monospecific stem cells. Throughout muscle growth, skeletal muscle modulates myosin isoforms like embryonic (MyHC-emb) and neonatal myosin heavy chains, respectively modulated from the myh3 and myh8 genes (50). These particular cytoskeletal motor proteins are transiently expressed during embryonic and fetal development and vanish after arrival when mature slow and fast myosins become widespread (51). After trauma or at neuromuscular disorders like DMD, developmental isoforms of myosin are re-expressed during muscle regeneration and also therefore are detected in recently formed regenerating myofibers 2-3 days following trauma and persist for 2-3 months. Therefore, the existence of the embryonic and neonatal cytoskeletal motor proteins represents a helpful markers of muscle regeneration along with a significant indicator of muscle damage, as amounts of cerebral myosin correlate with the clinical severity of Becker and DMD patients (55). Expression profiling from the authors demonstrated that MYH7b RNA is highly expressed in the heart, skeletal muscle, mature, and fetal brain and also much more slight expressed in the gut, kidney, liver, lung, liver, pancreas, and spleen 126 Since the human genome has been annotated, Desjardins et al. identified MYH7b as a member of three early myosins belonging to the sarcomeric myosin family of genes 17 MYH7b transcripts were verified in many conventional mammalian muscles such as the heart, soleus, tibialis anterior, quadriceps, and diaphragm 21, 127 A 2012 research by Warkman et al. reported that the existence of MYH7b protein from the mouse ; however, this finding was later amalgamated as that outcome was due to non invasive antibody reactivity 128 To date, MYH7b hasn’t yet been discovered at the protein level in mammalian cardiac or skeletal muscle.