ANTI-MYOSIN (SKELETAL AND SMOOTH)

Monoclonal Anti-Myosin (Skeletal, Slow) may be used for the localization of slow (Type I) myosin.
Monoclonal Anti-Myosin (Skeletal, Slow) antibody has been used in the detection of Myosin 7 using:

• light microscopy
• immunofluorescence staining
• immunoblotting
• ELISA
• solid-phase RIA
• immunohistology (frozen, formalin-fixed, paraffin-embedded and methacarn-fixed paraffin-embedded tissue sections)
• immunoelectronmicroscopy

Detection of slow myosin in formalin-fixed, paraffin-embedded, tissues is greatly enhanced by proteolytic digestion of the preparation.

Myosin is a 480 kDa protein known to interact with actin in muscle and in non-muscle cells. It contains two identical heavy chains (200 kDa each) and four light chains (15-26 kDa). Myosin 7 (MYH7) is mapped to human chromosome 14q11.1.
Monoclonal Anti-Myosin (Skeletal, Slow) (mouse IgG1 isotype) is derived from the NOQ7.5.4D hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. Myosin, purified from myofibrils isolated from human skeletal muscle, was used as the immunogen.1-3. The isotype is determined by a double diffusion immunoassay using Mouse Monoclonal Antibody Isotyping Reagents, Catalog Number ISO2.

Myosin molecules consist of two major regions: tail (rod) and heads; they aggregate into filaments through the tail region and interact with actin and with ATP through the head region. Multiple forms of myosin heavy chains exist for each muscle type: skeletal, cardiac, smooth and in non-muscle. Myosin isoforms exist in different types of skeletal muscle, depending on the physiological function of the muscle. Mammalian muscle fibers are classified primarily into slow (I), fast-red (IIa) and fast-white (IIb) major types. Changes in the speed of muscle contraction brought about by neural influences result from changes in the pattern of expression of myosin and other myofibrillar genes. Transient expression of different myosin isoforms occurs during fetal growth and development. Mutations in myosin 7 is associated with laing distal myopathy (LDM). Myosin 7 gene mutations results in muscular dystrophy diseases like scapuloperoneal myopathy. Mutations leads to storage of myosin protein aggregates in muscle, leading to myosin storage myopathy. Mutations in MYH7 is also associated with hypertrophic cardiomyopathy and in heart malformation disease called ebstein anomaly.