Human Heat Shock Protein 27 ELISA Kit (HSP27)

Supplementary info

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

Activity summary

Heat Shock Protein 27 (HSP27) also known as HSPB1 is a small heat shock protein with a molecular weight of approximately 27 kDa. It is expressed in various tissues including muscle heart and brain and responds to stress stimuli such as heat shock oxidative stress and inflammation. HSP27 functions as a molecular chaperone helping to stabilize unfolded proteins and prevent aggregation. Its expression increases significantly in cells undergoing stress playing a protective role in maintaining protein homeostasis.

Biological function summary

The small HSP protein functions in cellular processes like apoptosis cytoskeletal organization and protein folding. It does not act alone but often interacts with other proteins to form complexes that perform specific functions efficiently. HSP27 can bind to actin filaments influencing cell shape and motility. It also plays a role in preventing cell death by inhibiting apoptosome formation and modulating caspase activation. The dual role of protecting cells and modulating cell growth makes HSP27 an important tool for cells under stress.

Pathways

HSP27 interacts with the mitogen-activated protein kinase (MAPK) and PI3K/AKT signaling pathways. These pathways regulate cell survival growth and differentiation. Within these pathways HSP27 is linked to proteins such as Akt and MAPK which are critical for relaying survival and growth signals. By interacting with these molecules HSP27 helps to mediate the cell's response to external stressors and promotes cell survival under adverse conditions.

Associated diseases and disorders

HSP27 is significant in cancer and neurodegenerative diseases. Its overexpression often occurs in various cancers including breast and prostate cancer where it contributes to tumor growth and resistance to chemotherapy. In neurodegenerative diseases like Alzheimer's disease altered expression and functioning of HSP27 can lead to aggregation of proteins such as tau contributing to disease pathology. The link between HSP27 and these proteins shows its potential as a therapeutic target for modulating disease progression.