Heat Shock Protein 70 (HSP70) is a highly conserved molecular chaperone involved in protein folding, stabilization, and protection against cellular stress. Under conditions such as heat, hypoxia, oxidative stress, inflammation, or infection, HSP70 expression increases to help maintain protein homeostasis and prevent aggregation of misfolded proteins. Intracellular HSP70 supports cell survival by assisting in protein repair and regulating apoptosis, while extracellular HSP70—released during cellular stress or damage—can act as a signaling molecule within the immune system.
In research settings, HSP70 is widely studied as a marker of cellular stress, cytoprotection, and heat-shock response activation. Its expression levels are used to evaluate the impact of stressors, toxicants, therapeutic compounds, and disease models on cellular stability. Researchers also use HSP70 to study mechanisms of neurodegeneration, cancer progression, and immune activation, as it plays a role in antigen presentation and inflammatory signaling.
Clinically, HSP70 has emerging relevance as a potential biomarker for several conditions, including cancer, cardiovascular injury, autoimmune diseases, and neurodegenerative disorders. Elevated circulating HSP70 can indicate tissue damage, immune activation, or cellular stress, whereas tumor-associated HSP70 expression may correlate with prognosis, therapy resistance, and immune modulation. Although not yet mainstream in routine diagnostics, HSP70 is under investigation for its utility in risk stratification, early disease detection, and as a therapeutic target in oncology and inflammatory disorders.
This product is manufactured in Canada by StressMarq.
| Size | 1 x 96 Well |
| Sensitivity | 0.038 ng/mL |
| Dynamic Range | 0.42 – 27 ng/mL |
| Incubation Time | 30 minutes |
| Sample Type | Plasma, Cell Lysates, Tissue |
| Storage | 2-8°C (-20°C components) |
| Alternative Names | HSP70 1, HSP70 2, HSP70.1, HSP72, HSPA1, HSPA1A, HSPA1B |

