Recombinant Human Tropomyosin protein is a Human Full Length protein, in the 1 to 284 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, ELISA, WB, Dot.
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Binds to actin filaments in muscle and non-muscle cells (PubMed:23170982). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:23170982). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
C15orf13, TMSA, TPM1, Tropomyosin alpha-1 chain, Alpha-tropomyosin, Tropomyosin-1
Recombinant Human Tropomyosin protein is a Human Full Length protein, in the 1 to 284 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, ELISA, WB, Dot.
pH: 8
Constituents: 50% Glycerol (glycerin, glycerine), 0.32% Tris HCl
Binds to actin filaments in muscle and non-muscle cells (PubMed:23170982). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:23170982). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Belongs to the tropomyosin family.
Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.
Tropomyosin also known as anti-TM is a coiled-coil protein with a mass typically around 32 to 37 kDa depending on the isoform. This protein exists in both muscle and non-muscle cells playing essential roles in stabilizing actin filaments. In muscle tissues tropomyosin is part of the thin filament structure. It is found in high concentrations in skeletal cardiac and smooth muscles and is responsible for regulating the interaction between actin and myosin which is important for muscle contraction.
In muscle contraction and cellular movement tropomyosin acts as a regulatory protein. It associates with the troponin complex to control the binding of myosin heads to actin filaments. By shifting its position on the actin filament tropomyosin enables the muscle contraction cycle to proceed. It is an integral part of the thin filament complex interacting with actin and troponin and is essential for the calcium-dependent regulation of muscle contraction.
Tropomyosin plays a significant role in the actin cytoskeleton regulation pathway. It influences the dynamics of actin filament stability and organization which are important for cell motility and structure. The protein also interacts with the calmodulin-dependent protein kinase II (CaMKII) pathway where its interaction influences heart and skeletal muscle functionality. In these pathways tropomyosin regulates the activities of proteins such as myosin and actin ensuring proper cellular mechanical function and signaling.
Alterations in tropomyosin function can lead to several muscle-related conditions. Hypertrophic cardiomyopathy and dilated cardiomyopathy are two disorders associated with mutations in tropomyosin. In these conditions improper regulation of the actin-myosin interaction disrupts normal cardiac muscle function. Tropomyosin-related disorders often involve interactions with proteins such as troponin which is another key player in the regulation of muscle contraction and is important for maintaining a healthy cardiac rhythm.
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SDS-PAGE analysis of ab119162.
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