|Other Names||Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4|
|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||Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium.|
|Cellular Location||Cytoplasm, cytoskeleton.|
|Tissue Location||Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets of hypertensive patients without cardiac hypertrophy (at protein level).|
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This gene encodes a member of the tropomyosin family ofactin-binding proteins involved in the contractile system ofstriated and smooth muscles and the cytoskeleton of non-musclecells. Tropomyosins are dimers of coiled-coil proteins thatpolymerize end-to-end along the major groove in most actinfilaments. They provide stability to the filaments and regulateaccess of other actin-binding proteins. In muscle cells, theyregulate muscle contraction by controlling the binding of myosinheads to the actin filament. Multiple transcript variants encodingdifferent isoforms have been found for this gene. [provided byRefSeq].
Martins-de-Souza, D., et al. J Psychiatr Res 44(14):989-991(2010)Vlahovich, N., et al. Cell Motil. Cytoskeleton 65(1):73-85(2008)Montesano Gesualdi, N., et al. Free Radic. Res. 40(5):467-476(2006)Hossain, M.M., et al. J. Biol. Chem. 280(51):42442-42453(2005)Bruneel, A., et al. Proteomics 5(15):3876-3884(2005)
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