TRAP1 (Tumor necrosis factor receptor-associated protein 1), also known as HSP75. is a mitochondrial chaperone belonging to the heat shock protein 90 (HSP90) family. It plays a critical role in regulating cellular stress responses, oxidative phosphorylation, apoptosis, and metabolic reprogramming. TRAP1 is structurally distinct from cytosolic HSP90 due to its N-terminal mitochondrial targeting sequence and unique ATP-binding domain. Studies have linked TRAP1 to cancer progression, as it promotes tumor cell survival under hypoxic or drug-treated conditions by inhibiting mitochondrial permeability transition pore opening and cytochrome c release.
TRAP1 antibodies are essential tools for studying its expression, localization, and function in both physiological and pathological contexts. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to investigate TRAP1's role in diseases, particularly cancers. Commercial TRAP1 antibodies are typically raised against specific epitopes, such as the N-terminal or ATPase domains, with validation across species including human, mouse, and rat. Researchers have observed TRAP1 overexpression in various cancers, including colorectal, prostate, and ovarian cancers, suggesting its potential as a therapeutic target or biomarker. However, antibody specificity remains a challenge, requiring careful validation using knockout controls or siRNA-mediated silencing. Recent interest in TRAP1 inhibitors for anticancer therapy has further driven the demand for reliable antibodies to assess target engagement and treatment efficacy.