HSP90AA1 Antibody / HSP90 alpha [clone CCF-8] (RQ5193)

HSP90AA1 Antibody WB. Western blot analysis of human HeLa cell lysate using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates a strong immunoreactive band at approximately 86-90 kDa, consistent with the predicted molecular weight of HSP90AA1. HSP90AA1 (HSP90 alpha) is a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and maintenance of cellular homeostasis. As one of the most abundant intracellular chaperones, HSP90AA1 plays essential roles in proteostasis, cellular stress responses, and regulation of numerous signaling pathways. The observed band supports detection of HSP90AA1 in human cells by western blot analysis. Predicted molecular weight: approximately 86-90 kDa.

HSP90AA1 Antibody Breast Cancer IHC. Immunohistochemistry staining of FFPE human breast cancer tissue using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates moderate cytoplasmic HRP-DAB brown staining within malignant epithelial tumor cells. The staining pattern is consistent with expression of HSP90AA1 (HSP90 alpha), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and maintenance of cellular homeostasis. HSP90AA1 supports the activity of numerous signaling molecules involved in cellular proliferation, survival, and adaptation to tumor-associated stress, making it an important target in cancer biology and proteostasis research. HIER was performed by boiling tissue sections in pH 6, 10 mM citrate buffer for 10-20 minutes followed by cooling prior to immunostaining.