The HSPA9 antibody is a crucial tool for studying the HSPA9 protein, a member of the heat shock protein 70 (HSP70) family. HSPA9. also known as GRP75 or mortalin, is a mitochondrial chaperone involved in protein folding, mitochondrial protein import, and stress response. It plays essential roles in maintaining mitochondrial function, regulating apoptosis, and supporting cellular homeostasis. Dysregulation of HSPA9 has been linked to various diseases, including cancer, neurodegenerative disorders (e.g., Alzheimer’s and Parkinson’s), and metabolic syndromes.
The HSPA9 antibody enables researchers to detect and quantify HSPA9 expression in tissues or cell lines using techniques like Western blotting, immunofluorescence, and immunohistochemistry. It also aids in studying its subcellular localization, interactions with client proteins (e.g., p53. telomerase), and involvement in mitochondrial dynamics. Commercial HSPA9 antibodies are typically raised against specific epitopes, such as the N-terminal or C-terminal regions, and validated for cross-reactivity across species (human, mouse, rat).
Research using HSPA9 antibodies has revealed its dual role in cancer—acting as both a tumor suppressor and promoter depending on context—and its association with chemoresistance. In neurodegeneration, HSPA9 depletion correlates with mitochondrial dysfunction and protein aggregation. As a biomarker or therapeutic target, HSPA9 remains under investigation, highlighting the antibody's importance in mechanistic and translational studies.