HSP90AA1 Antibody / Molecular Chaperone Antibody [clone 6B5] (RQ6535)

HSP90AA1 Antibody IF. Immunofluorescent staining of FFPE human SiHa cells using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates strong cytoplasmic green fluorescence with minimal nuclear staining. The staining pattern is consistent with expression of HSP90AA1 (HSP90a), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. HSP90AA1 is one of the most abundant intracellular chaperones and plays a central role in maintaining proteostasis and cellular homeostasis. HIER was performed by steaming sections in pH 6 citrate buffer for 20 minutes prior to staining. HSP90AA1 was detected with a green fluorophore, while nuclei were counterstained with DAPI (blue).

HSP90AA1 Antibody Colon Cancer IHC. Immunohistochemistry staining of FFPE human colon cancer tissue using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates strong cytoplasmic HRP-DAB brown staining within malignant gland-forming epithelial cells. The staining pattern is consistent with expression of HSP90AA1 (HSP90a), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. HSP90AA1 supports the function of numerous signaling molecules involved in cellular growth, survival, and tumor progression, making it an important target in cancer biology and proteostasis research. HIER was performed by boiling tissue sections in pH 8 EDTA buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90AA1 Antibody Cervical Cancer IHC. Immunohistochemistry staining of FFPE human cervical cancer tissue using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates strong cytoplasmic HRP-DAB brown staining within malignant epithelial cells. The staining pattern is consistent with expression of HSP90AA1 (HSP90a), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. HSP90AA1 supports the activity of numerous proteins involved in cellular proliferation, survival, and adaptation to physiological stress, making it an important target in cancer biology and proteostasis research. HIER was performed by boiling tissue sections in pH 8 EDTA buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90AA1 Antibody Lung Cancer IHC. Immunohistochemistry staining of FFPE human lung 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 (HSP90a), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. HSP90AA1 supports the activity of numerous regulatory proteins 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 8 EDTA buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90AA1 Antibody Testis Cancer IHC. Immunohistochemistry staining of FFPE human testis cancer tissue using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates cytoplasmic HRP-DAB brown staining within malignant tumor cells. The staining pattern is consistent with expression of HSP90AA1 (HSP90a), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. HSP90AA1 supports the activity of numerous proteins involved in cellular proliferation, survival, and adaptation to physiological stress, making it an important target in cancer biology, proteostasis research, and studies of tumor-associated signaling networks. HIER was performed by boiling tissue sections in pH 8 EDTA buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90AA1 Antibody WB. Western blot analysis of human HeLa (lane 1), human HEK293 (lane 2), monkey COS-7 (lane 3), human HepG2 (lane 4), human A549 (lane 5), rat PC-3 (lane 6), rat RH35 (lane 7), and mouse HEPA1-6 (lane 8) cell lysates using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates a prominent immunoreactive band at approximately 86-90 kDa across multiple mammalian cell lines. 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 cellular stress-response pathways. HSP90AA1 is ubiquitously expressed in many cell types and plays essential roles in maintaining proteostasis and cellular homeostasis. The observed cross-species reactivity supports detection of HSP90AA1 in human, monkey, rat, and mouse samples by western blot analysis. Predicted molecular weight: approximately 86-90 kDa.

HSP90AA1 Antibody FACS. Flow cytometry analysis of human A549 cells using HSP90AA1 Antibody / Molecular Chaperone Antibody demonstrates a clear rightward shift of the antibody-stained population (blue) relative to the isotype control (green) and unstained cells (red), consistent with detection of HSP90AA1 expression. HSP90AA1 (HSP90 alpha) is a highly conserved ATP-dependent molecular chaperone involved in protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. Due to its central role in maintaining proteostasis and cellular homeostasis, HSP90AA1 is widely studied in cancer biology, cell signaling, and stress-response research. Cells were stained with HSP90AA1 antibody at 1 ug/million cells following blocking with goat sera. Red = cells alone, Green = isotype control, Blue = HSP90AA1 antibody.