TPM2 Human

Tropomyosin-2, also known as TPM2, is a protein that plays a crucial role in muscle contraction and cytoskeletal functions. It is a member of the actin filament binding protein family and is predominantly expressed in slow, type 1 muscle fibers. The recombinant form of this protein, known as Tropomyosin-2 (Human Recombinant), is produced using recombinant DNA technology, which allows for the expression of the protein in a host organism such as Escherichia coli.

Tropomyosin-2 is composed of 284 amino acids and has a molecular weight of approximately 35.1 kDa. The protein is characterized by its ability to bind along the length of actin filaments, stabilizing them and regulating their interactions with other proteins. This binding is essential for the proper functioning of muscle contraction and other cellular processes that involve the cytoskeleton.

The recombinant form of Tropomyosin-2 is typically produced in Escherichia coli. The gene encoding the protein is inserted into a plasmid vector, which is then introduced into the bacterial cells. The bacteria are cultured under conditions that promote the expression of the recombinant protein. Once expressed, the protein is purified using conventional chromatography techniques to achieve a purity of over 90% .

Recombinant Tropomyosin-2 is used in various research applications, including studies on muscle physiology, cytoskeletal dynamics, and protein-protein interactions. It is also used in the investigation of diseases associated with mutations in the TPM2 gene, such as cap disease, nemaline myopathy, and distal arthrogryposis syndromes .

Mutations in the TPM2 gene can lead to a range of muscle disorders. These mutations can alter the expression and function of Tropomyosin-2, resulting in conditions such as cap disease, nemaline myopathy, and distal arthrogryposis syndromes. Understanding the structure and function of Tropomyosin-2 is therefore critical for developing therapeutic strategies for these diseases .