TPM1 (tropomyosin 1 (alpha))

Polyclonal antibody produced in rabbits immunized with a synthetic peptide corresponding to a region of Human TPM1.

Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. TPM1 is a member of the tropomyosin family of highly conserved. widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-heli

Heterodimer of an alpha and a beta chain.

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity. Mass Spectrometry: Mass=32875. 93; Method=MALDI; Range=1-284 (P09493-3); Source=PubMed:11840567; .

Belongs to the tropomyosin family. Summary: This protein is a member of the tropomyosin family of highly conserved widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy. Lin. J. C. (2005) Mol. Cell. Biol. 25 (22). 10111-10121.