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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 (MYOM1) and 165 kD (MYOM2). Sequence analysis indicated that the predicted MYOM1 protein contains 1,451 amino acids and has a molecular mass of 162 kD, somewhat lower than the apparent mass of 190 kD. Like the 165-kD protein, titin, and other myofibrillar proteins, the MYOM1 contains structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. MYOM1 and the 165-kD protein 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 2 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.
Gene Name: | myomesin 1 |
Synonyms: | MYOM1, EH-myomesin, Myomesin 1 (skelemin) 185kDa, Myomesin (M-protein) 1 (190kD), Myomesin 1 (skelemin) (185kD), Myomesin 1, 185kDa, Myomesin family member 1, Myomesin-1, SKELEMIN, Myomesin, Myomesin 1 |
Target Sequences: | NM_003803 NP_003794.3 P52179 |
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