Titin N-Fragment (Serum) ELISA (Human)
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Solid phase sandwich ELISA designed for the determination of Titin N fragment in human serum. For research use only, not for use in diagnostic procedures. <br> <br>
Titin (connectin) is a protein that consists of 34,350 amino-acid and specifically expresses in a cross-striated muscle. The molecular weight of human titin is 3,816 kDa and it has been known that as the largest protein among the existing proteins in a living body.
It is one of sarcomere structured protein that is a minimum unit of myofibrillary protein and it has a role as an elastic protein for recovering the length of shortened sarcomere by its contraction. It has been known that titin is cleaved by protein metabolic enzymes such as calpain and matrix metalloprotease if muscles are damaged.
Titin degradation was observed in the skeletal muscle related to muscular dystrophy, and the presence of various titin fragments in the blood and urine was confirmed. In particular, it has been reported that the approximately 26 kDa N-fragment on the N-terminal region and the approximately 12 kDa C-fragment on the C-terminal region found in urine are increased in various muscle problems including muscular dystrophy.
Titin has been researched in the field of sports medicine, cardiac disease, NAFLD, sarcopenia and frailty and it is also considered that it can be a candidate as a non-invasive biomarker for monitoring status of muscles.
Solid phase sandwich ELISA designed for the determination of Titin N fragment in human serum. For research use only, not for use in diagnostic procedures. <br> <br>
Titin (connectin) is a protein that consists of 34,350 amino-acid and specifically expresses in a cross-striated muscle. The molecular weight of human titin is 3,816 kDa and it has been known that as the largest protein among the existing proteins in a living body.
It is one of sarcomere structured protein that is a minimum unit of myofibrillary protein and it has a role as an elastic protein for recovering the length of shortened sarcomere by its contraction. It has been known that titin is cleaved by protein metabolic enzymes such as calpain and matrix metalloprotease if muscles are damaged.
Titin degradation was observed in the skeletal muscle related to muscular dystrophy, and the presence of various titin fragments in the blood and urine was confirmed. In particular, it has been reported that the approximately 26 kDa N-fragment on the N-terminal region and the approximately 12 kDa C-fragment on the C-terminal region found in urine are increased in various muscle problems including muscular dystrophy.
Titin has been researched in the field of sports medicine, cardiac disease, NAFLD, sarcopenia and frailty and it is also considered that it can be a candidate as a non-invasive biomarker for monitoring status of muscles.