Anti-HSPA14 antibody [EPR4210]

Supplementary info

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

Activity summary

The target HSPA14 also known as Heat Shock Protein Family A Member 14 acts as a chaperone protein involved in protein folding and proteostasis within cells. HSPA14 has a molecular weight of approximately 54 kDa. It is expressed in a variety of tissues with notable presence in skeletal muscle heart and brain. The high expression in these areas suggests a significant role in managing cellular stress and maintaining proper protein function especially under conditions that can lead to protein misfolding.

Biological function summary

HSPA14 plays a significant role in the heat shock response which protects cells from damage caused by elevated temperatures and other stressors. It is part of a larger complex interacting with other molecular chaperones and co-chaperones to efficiently facilitate the refolding or degradation of misfolded proteins. This action helps to preserve cellular homeostasis and prevent aggregation that can disrupt cell function.

Pathways

HSPA14 contributes to the unfolded protein response and protein quality control systems. It connects with pathways like the heat shock signaling pathway influencing the expression and activation of other heat shock proteins. In particular its interactions with proteins such as HSP70 and HSP90 highlight its role in maintaining protein stability and stress resilience in the cell.

Associated diseases and disorders

HSPA14 shows links to neurodegenerative diseases and certain types of cancer. For instance misregulation of HSPA14 has associations with Alzheimer's disease due to its role in managing protein aggregation. Additionally its connections with proteins such as tau which is implicated in neurodegeneration indicate the potential impact of HSPA14 dysregulation. In cancer alterations in HSPA14 expression might influence tumor progression by affecting stress responses and cell survival mechanisms.