Alexa Fluor® 568 Anti-HSPA4 抗体 [EPR14165]

補足情報

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

HSPA4 also known as Heat Shock Protein Family A Member 4 is a molecular chaperone involved in protein folding and stabilization during stress. This protein belongs to the heat shock protein family and has a molecular weight of approximately 70 kDa. HSPA4 is widely expressed across various tissues including the heart liver and brain. It operates within the cytoplasm and nucleus where it assists in protein homeostasis by preventing aggregation and misfolding of nascent polypeptides.

Biological function summary

HSPA4 plays a role in cellular stress responses and is part of the HSP70 chaperone complex. HSPA4 interacts with co-chaperones and other proteins to facilitate proper protein folding and degradation. It assists in the recovery of cells from thermal and oxidative stress. The protein ensures the stability of essential signal transduction proteins and supports protein quality control systems within the cell.

Pathways

HSPA4 integrates into the cellular stress response and protein degradation pathways. It engages with the ubiquitin-proteasome system aiding in the removal of damaged proteins. HSPA4 interacts with other heat shock proteins such as HSPA1A and HSPA5 coordinating stress response signals and maintaining cellular homeostasis. This involvement in protein maintenance links it to regulatory pathways that address protein misfolding and cellular repair processes.

HSPA4 shows connections to neurodegenerative diseases and cancer. Its role in protein homeostasis suggests involvement in Alzheimer's disease as protein misfolding stands as an important pathological feature. In cancer HSPA4 is associated with cell proliferation and survival mechanisms. It interacts with oncogene products potentially contributing to tumor progression. Studies explore HSPA4 as a therapeutic target assessing its potential influence in disease modulation through its interactions with other stress proteins and pathways.