HSP90 alpha Antibody / Heat Shock Protein 90 Alpha Antibody (R31907)

HSP90 alpha 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-12 (lane 6), rat RH35 (lane 7), and mouse HEPA1-6 (lane 8) cell lysates using HSP90 alpha Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates a prominent immunoreactive band at approximately 86-90 kDa across multiple mammalian cell lines. The staining pattern is consistent with expression of HSP90 alpha (HSP90AA1), a highly conserved ATP-dependent molecular chaperone involved in protein folding, stabilization of client proteins, signal transduction, and maintenance of cellular homeostasis. HSP90 alpha is ubiquitously expressed and plays essential roles in proteostasis, stress-response pathways, and regulation of numerous signaling proteins. The observed cross-species reactivity supports detection of HSP90 alpha in human, monkey, rat, and mouse samples by western blot analysis. Predicted molecular weight: approximately 86-90 kDa.

HSP90 alpha Antibody Testis IHC. Immunohistochemistry staining of FFPE human testis using HSP90 alpha Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates strong cytoplasmic HRP-DAB brown staining within seminiferous tubule germ cell populations. The staining pattern is consistent with expression of HSP90 alpha (HSP90AA1), a highly conserved ATP-dependent molecular chaperone involved in protein folding, stabilization of client proteins, cellular stress responses, and maintenance of proteostasis. HSP90 alpha is highly expressed in metabolically active and proliferative cell populations, where it supports the maturation and function of numerous signaling and regulatory proteins. HIER was performed by boiling paraffin sections in pH 6, 10 mM citrate buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90 alpha Antibody Mouse Testis IHC. Immunohistochemistry staining of FFPE mouse testis using HSP90 alpha Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates strong cytoplasmic HRP-DAB brown staining within seminiferous tubule germ cell populations. The staining pattern is consistent with expression of HSP90 alpha (HSP90AA1), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, cellular stress responses, and maintenance of proteostasis. HSP90 alpha is highly expressed in developing germ cells and other metabolically active cell populations, where it supports the function of signaling proteins required for cellular growth, differentiation, and survival. HIER was performed by boiling paraffin sections in pH 6, 10 mM citrate buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90 alpha Antibody Rat Testis IHC. Immunohistochemistry staining of FFPE rat testis using HSP90 alpha Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates strong cytoplasmic HRP-DAB brown staining within seminiferous tubule germ cell populations. The staining pattern is consistent with expression of HSP90 alpha (HSP90AA1), a highly conserved ATP-dependent molecular chaperone involved in protein folding, stabilization of client proteins, cellular stress responses, and maintenance of proteostasis. HSP90 alpha supports the maturation and function of numerous signaling proteins required for germ cell development, differentiation, and survival. HIER was performed by boiling paraffin sections in pH 6, 10 mM citrate buffer for 20 minutes followed by cooling prior to immunostaining.

HSP90 alpha Antibody IF. Immunofluorescent staining of FFPE human U-2 OS cells using HSP90 alpha Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates strong cytoplasmic red fluorescence with relative exclusion from the nucleus. The staining pattern is consistent with expression of HSP90 alpha (HSP90AA1), a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. HSP90 alpha is predominantly localized within the cytoplasm, where it maintains proteostasis and supports the activity of numerous signaling and regulatory proteins. HIER was performed by steaming sections in pH 6 citrate buffer for 20 minutes prior to staining. HSP90 alpha was detected with a red fluorophore, while nuclei were counterstained with DAPI (blue).

HSP90 alpha Antibody FACS. Flow cytometry analysis of human SiHa cells using HSP90 alpha Antibody / Heat Shock Protein 90 Alpha 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 HSP90 alpha expression. HSP90 alpha (HSP90AA1) is a highly conserved ATP-dependent molecular chaperone that regulates protein folding, stabilization of client proteins, signal transduction, and cellular stress-response pathways. As a central component of the cellular proteostasis network, HSP90 alpha supports the activity of numerous signaling and regulatory proteins involved in cellular growth, survival, and adaptation to physiological stress. Cells were stained with HSP90 alpha antibody at 1 ug/million cells following blocking with goat sera. Red = cells alone, Green = isotype control, Blue = HSP90 alpha antibody.