Anti-Hsp20 antibody [EPR14457] - BSA and Azide free

Supplementary info

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

Activity summary

Hsp20 also known as Heat Shock Protein 20 or HspB6 is a small heat shock protein with a molecular weight of approximately 20 kDa. It functions by binding to partially unfolded proteins preventing them from aggregating and assisting in their proper folding. Hsp20 achieves this through its chaperone activity similar to other small heat shock proteins. This protein is expressed ubiquitously with high levels found in cardiac and skeletal muscles as well as in the brain and placenta.

Biological function summary

The small heat shock protein family which includes Hsp20 plays a critical role in maintaining cellular proteostasis under stress conditions. Hsp20 does not typically form large complexes though it may oligomerize under certain conditions to exert its protective functions. It interacts with cellular structures and proteins to maintain cell integrity and function. Hsp20 can modulate actin filament dynamics influencing cellular motility and smooth muscle relaxation.

Pathways

The Hsp20 protein is actively involved in several key regulatory pathways. It plays a role in the stress response pathway and is engaged in the cardiomyocyte signaling network. Hsp20 interacts closely with proteins such as Akt and PKA which are involved in the signaling cascades that govern cell survival and response to stress. Phosphorylation of Hsp20 by PKA contributes to its protective functions especially in cardiac tissues.

Associated diseases and disorders

Alterations in Hsp20 expression or function can impact the development of cardiac diseases and neurodegenerative disorders. The protein is associated with cardiomyopathies where its protective role is important in managing stress in cardiac cells. Furthermore changes in Hsp20 have implications for Alzheimer's disease due to its interactions with tau protein. Enhanced understanding of Hsp20's mechanisms might lead to better therapeutic strategies for these diseases.