|Other Names||Myomesin-1, 190 kDa connectin-associated protein, 190 kDa titin-associated protein, Myomesin family member 1, MYOM1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13444c was selected from the Center region of MYOM1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.|
|Cellular Location||Cytoplasm, myofibril, sarcomere, M line|
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Provided below are standard protocols that you may find useful for product applications.
The giant protein titin, together with its associatedproteins, interconnects the major structure of sarcomeres, the Mbands and Z discs. The C-terminal end of the titin string extendsinto the M line, where it binds tightly to M-band constituents ofapparent molecular masses of 190 kD (myomesin 1) and 165 kD(myomesin 2). This protein, myomesin 1, like myomesin 2, titin, andother myofibrillar proteins contains structural modules with stronghomology to either fibronectin type III (motif I) or immunoglobulinC2 (motif II) domains. Myomesin 1 and myomesin 2 each have a uniqueN-terminal region followed by 12 modules of motif I or motif II, inthe arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteinsshare 50% sequence identity in this repeat-containing region. Thehead structure formed by these 2 proteins on one end of the titinstring extends into the center of the M band. The integratingstructure of the sarcomere arises from muscle-specific members ofthe superfamily of immunoglobulin-like proteins. Alternativelyspliced transcript variants encoding different isoforms have beenidentified.
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Schoenauer, R., et al. J. Mol. Biol. 349(2):367-379(2005)Hornemann, T., et al. J. Mol. Biol. 332(4):877-887(2003)Porter, J.D., et al. J. Exp. Biol. 206 (PT 17), 3101-3112 (2003) :Agarkova, I., et al. J. Biol. Chem. 275(14):10256-10264(2000)
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