|Other Names||Tropomodulin-1, Erythrocyte tropomodulin, E-Tmod, TMOD1, D9S57E, TMOD|
|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||Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus.|
|Cellular Location||Cytoplasm, cytoskeleton. Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments (PubMed:25250574).|
|Tissue Location||Highly expressed in the erythrocyte, heart and skeletal muscle|
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TMOD1 is a member of the tropomodulin family. Theencoded protein is an actin-capping protein that regulatestropomyosin by binding to its N-terminus, inhibitingdepolymerization and elongation of the pointed end of actinfilaments and thereby influencing the structure of the erythrocytemembrane skeleton. Multiple transcript variants encoding the sameprotein have been found for this gene.
Olsen, J.V., et al. Cell 127(3):635-648(2006)Kong, K.Y., et al. J. Biol. Chem. 281(14):9589-9599(2006)Vera, C., et al. Arch. Biochem. Biophys. 444(2):130-138(2005)Pawlak, G., et al. Int. J. Cancer 110(3):368-373(2004)Rho, S.B., et al. FEBS Lett. 557 (1-3), 57-63 (2004) :
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