The MYOM1 Polyclonal Antibody (PAC013525) is a valuable tool for researchers studying MYOM1, a protein involved in muscle function and structure. This antibody, produced in rabbits, exhibits high reactivity with human samples and is validated for use in Western blot applications. By binding specifically to the MYOM1 protein, this antibody enables precise detection and analysis in various cell types, making it ideal for investigations in muscle biology and related research fields.MYOM1, also known as myomesin-1, is a key player in muscle development and contraction, contributing to the organization and stability of sarcomeres.
Its role in maintaining muscle integrity and function highlights its importance in understanding conditions such as muscular dystrophy, myopathies, and muscle disorders. Research on MYOM1 provides insights into muscle physiology and pathophysiology, paving the way for potential therapeutic interventions targeting muscle-related diseases.
myomesin 1: Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent. 2 isoforms of the human protein are produced by alternative splicing.Protein type: CytoskeletalChromosomal Location of Human Ortholog: 18p11.31Cellular Component: M band; striated muscle thick filamentMolecular Function: identical protein binding; protein binding; protein homodimerization activity; structural constituent of muscleBiological Process: positive regulation of defense response to virus by host
UniProt Protein Details:
NCBI Summary:
The giant protein titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to M-band constituents of apparent molecular masses of 190 kD (myomesin 1) and 165 kD (myomesin 2). This protein, myomesin 1, like myomesin 2, titin, and other myofibrillar proteins contains structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. Myomesin 1 and myomesin 2 each have a unique N-terminal region followed by 12 modules of motif I or motif II, in the arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteins share 50% sequence identity in this repeat-containing region. The head structure formed by these 2 proteins on one end of the titin string extends into the center of the M band. The integrating structure of the sarcomere arises from muscle-specific members of the superfamily of immunoglobulin-like proteins. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]
