Anti-TPM4 antibody [EPR13317] - BSA and Azide free

Supplementary info

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

Activity summary

TPM4 also known as tropomyosin 4 or TM4 is a protein that helps regulate muscle contraction and stabilize actin filaments. It has a molecular mass of approximately 28 kDa. TPM4 expression occurs in various tissues including both skeletal and smooth muscle tissues as well as in non-muscle cells. This protein is part of a larger family of tropomyosins which bind to actin filaments and play an important role in modulating actin's interaction with other proteins.

Biological function summary

TPM4 contributes to the regulation of the actin cytoskeleton dynamics influencing cell movement and shape. TPM4 like other tropomyosins associates with actin filaments and forms a part of a complex with other actin-binding proteins such as tropomodulins. This complex is critical in both maintaining filament stability and facilitating the sliding of actin filaments during muscle contraction and other cellular activities.

Pathways

TPM4 participates actively in the cytoskeletal signaling and muscle contraction pathways. It interacts with important components in these pathways such as myosin allowing coordinated muscle contractions. TPM4 also plays a role in the regulation of the RhoA signaling pathway which is connected to cytoskeletal rearrangement and cell motility. These interactions highlight TPM4's integral position in biological processes relying on actin filament dynamics.

Associated diseases and disorders

Misregulation of TPM4 can influence the development of conditions such as cardiomyopathies and cancer. Alterations in its expression or function may link to familial hypertrophic cardiomyopathy where it interacts with cardiac-specific proteins like cardiac myosin heavy chain (MYH7). Furthermore changes in TPM4 expression levels may associate with cancer metastasis in part due to its role in cell motility and invasion pointing to potential connections with proteins like cofilin during cancer progression.