Recombinant Proteins
Product List
TPM1 Human
Tropomyosin-1 Human Recombinant
TPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 304 amino acids (1-284 a.a.) and having a total molecular mass of 35kDa (Molecular weight on SDS-PAGE will appear higher).
TPM1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
TPM2 Human
Tropomyosin-2 Human Recombinant
TPM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
TPM3 Human
Tropomyosin-3 Human Recombinant
TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
TPM4 Human
Tropomyosin-4 Human Recombinant
TPM4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Tropomyosin is a two-stranded alpha-helical, coiled-coil protein found in many animal and fungal cells . It is a critical component of the actin cytoskeleton, playing a vital role in muscle contraction and stabilization of the cytoskeleton . Tropomyosins are categorized into two main groups: muscle tropomyosin isoforms and nonmuscle tropomyosin isoforms . Muscle isoforms regulate interactions between actin and myosin in muscle sarcomeres, while nonmuscle isoforms function in various cellular pathways .
Tropomyosin is expressed in smooth and striated muscle tissues, including the heart, blood vessels, respiratory system, and digestive system . It is also found in nonmuscle cells, where it regulates the actin cytoskeleton . Tropomyosin isoforms exhibit tissue-specific expression patterns, with different isoforms present in various organs and body systems . For example, TPM3 gene expression can be detected in skeletal muscle, endothelial cells, and neurons .
Tropomyosin’s primary function is to regulate muscle contraction by controlling the interaction between actin and myosin . It also plays a role in stabilizing the cytoskeleton in nonmuscle cells . Tropomyosin is involved in immune responses and pathogen recognition by modulating the actin cytoskeleton, which is crucial for cell motility and phagocytosis .
Tropomyosin binds along the length of actin filaments, blocking myosin-binding sites in the absence of a nerve impulse . Upon calcium ion release, tropomyosin undergoes a conformational change, exposing the myosin-binding sites and allowing muscle contraction . Tropomyosin interacts with various actin-binding proteins, including troponin, caldesmon, and gelsolin, to regulate actin filament stability and function .
The expression and activity of tropomyosin are regulated through transcriptional and post-translational mechanisms . Alternative splicing of tropomyosin genes generates multiple isoforms with distinct functions . Post-translational modifications, such as phosphorylation, also play a role in modulating tropomyosin’s interaction with actin and other binding partners .
Tropomyosin has several applications in biomedical research, including its use as a biomarker for various cancers . It is also studied for its role in muscle diseases and as a potential therapeutic target for conditions involving cytoskeletal dysfunction . Tropomyosin’s involvement in actin dynamics makes it a valuable tool for understanding cell motility and morphology .
Tropomyosin plays a crucial role throughout the life cycle, from development to aging and disease . During development, tropomyosin isoforms contribute to the formation and function of muscle tissues . In aging, changes in tropomyosin expression and function can lead to muscle weakness and other age-related conditions . Tropomyosin is also implicated in various diseases, including congenital myopathies and cancer .
