The HSPA1A antibody targets the HSPA1A protein, a member of the heat shock protein 70 (HSP70) family, also known as HSP72 or HSP70-1. Encoded by the *HSPA1A* gene, this protein functions as a molecular chaperone, assisting in protein folding, preventing aggregation under stress, and facilitating the degradation of misfolded proteins. It is highly inducible in response to cellular stressors like heat shock, oxidative stress, or toxins, playing a critical role in maintaining proteostasis and cell survival.
HSPA1A antibodies are widely used in research to study the heat shock response, cellular stress pathways, and diseases linked to protein misfolding, such as cancer, neurodegenerative disorders (e.g., Alzheimer’s, Parkinson’s), and inflammatory conditions. These antibodies enable detection of HSPA1A expression via techniques like Western blotting, immunohistochemistry, ELISA, and flow cytometry. Specificity is crucial due to high homology among HSP70 family members; thus, antibodies are often validated against recombinant proteins or knockout cells.
In disease contexts, HSPA1A is implicated in both protective and pathological roles. For example, it supports cancer cell survival under hypoxia or chemotherapy, making it a potential therapeutic target. Conversely, its dysregulation may contribute to neurotoxicity in proteinopathies. Research using HSPA1A antibodies helps clarify its dual functions, guiding drug development and biomarker discovery. Commercial antibodies vary in host species, clonality, and conjugation, allowing flexibility in experimental design. Proper controls are essential to ensure accurate interpretation, given the protein’s stress-inducible nature and ubiquitous expression.