Anti-Tropomyosin 2 antibody [EPR12846] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Tropomyosin 2 (TPM2) is a protein that plays an important mechanical role in muscle function. It is a component of the actin filament system weighing approximately 32.7 kDa. TPM2 interacts with actin to stabilize the filament structures which are essential in muscle contraction processes. This protein is expressed mainly in muscle tissues including skeletal and cardiac muscles but is also present in other tissues. Its stability and interaction with actin filaments make it significant in maintaining sarcomere structure.

Biological function summary

TPM2 ensures proper muscle contraction by regulating the interaction between actin and myosin two key components in muscle movement. It forms a complex with actin and troponin a critical protein that regulates muscle contraction through calcium ion binding. This complex facilitates muscle fiber contraction by exposing the binding sites for myosin on actin filaments. The presence of TPM2 in the complex is essential for the contraction mechanism allowing precise control of muscle movements.

Pathways

TPM2 acts in the regulation of muscle contraction and actin cytoskeleton signaling pathways. In the muscle contraction pathway TPM2 interacts closely with tropomyosin 1 (TPM1) and the myosin motor protein playing a regulatory role. It is involved in the actin cytoskeleton signaling pathway where it helps organize actin filaments necessary for various cellular activities. Through these pathways TPM2 integrates signals essential for muscle activity and cellular architecture maintenance.

Associated diseases and disorders

TPM2 mutations have a notable connection to conditions such as nemaline myopathy and distal arthrogryposis. Nemaline myopathy is characterized by muscle weakness and it arises due to defects in sarcomere proteins with TPM2 being a significant player. Additionally changes in TPM2 can associate with contractures and joint deformities in distal arthrogryposis. The protein connects to cellular disorders through its interactions with troponin I (TNNI2) and other structural sarcomere components highlighting its critical role in muscle integrity and function.