Zebrafish HSP90AA1 Antibody / Heat Shock Protein 90 Alpha Antibody (RZ1397)

Zebrafish HSP90AA1 Antibody IF. Immunofluorescent staining of paraffin-embedded zebrafish embryo tissue using Zebrafish HSP90AA1 Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates widespread green fluorescence throughout developing embryonic tissues. The staining pattern is consistent with expression of HSP90A, a highly conserved molecular chaperone orthologous to human HSP90AA1 (heat shock protein 90 alpha family class A member 1). HSP90A functions in protein folding, stabilization of signaling proteins, cellular stress responses, and maintenance of proteostasis, making it essential for normal embryonic development and tissue homeostasis. HIER was performed in pH 8.0 EDTA buffer prior to staining. Tissue sections were blocked with 10% goat serum and incubated with primary antibody at 5 ug/ml overnight at 4°C. DyLight®488-conjugated goat anti-rabbit IgG was used as the secondary antibody (green), and nuclei were counterstained with DAPI (blue). The image supports detection of HSP90A expression in developing zebrafish embryonic tissues by immunofluorescence.

Zebrafish HSP90AA1 Antibody Cardiac Tissue IHC. Immunohistochemical analysis of paraffin-embedded zebrafish cardiac tissue using Zebrafish HSP90AA1 Antibody demonstrates cytoplasmic HRP-DAB brown staining within cells and tissue structures of the heart region. HSP90AA1 is a molecular chaperone involved in protein folding, stress responses, signal transduction, and maintenance of cellular proteostasis. Positive staining is observed in cardiac-associated tissue containing abundant blood cells, consistent with the widespread expression of HSP90AA1 in metabolically active vertebrate tissues. Heat-induced antigen retrieval was performed in EDTA buffer prior to incubation with HSP90AA1 antibody (2 ug/ml) and DAB detection.

Zebrafish HSP90AA1 Antibody Brain IHC. Immunohistochemistry staining of paraffin-embedded zebrafish brain tissue using Zebrafish HSP90AA1 Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates widespread cytoplasmic HRP-DAB brown staining within neural tissue-associated cellular populations. The staining pattern is consistent with expression of HSP90A, a highly conserved molecular chaperone orthologous to human HSP90AA1 (heat shock protein 90 alpha family class A member 1). HSP90A functions in protein folding, stabilization of signaling proteins, cellular stress responses, and maintenance of proteostasis, making it an important regulator of neuronal homeostasis and developmental signaling pathways. HIER was performed in pH 8.0 EDTA buffer. Tissue sections were blocked with 10% goat serum and incubated with primary antibody at 2 ug/ml overnight at 4°C prior to detection with HRP-conjugated secondary antibody and DAB chromogen.

Zebrafish HSP90AA1 Antibody Muscle IHC. Immunohistochemistry staining of paraffin-embedded zebrafish muscle tissue using Zebrafish HSP90AA1 Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates strong cytoplasmic HRP-DAB brown staining within striated muscle fibers. The staining pattern is consistent with expression of HSP90A, a highly conserved molecular chaperone orthologous to human HSP90AA1 (heat shock protein 90 alpha family class A member 1). HSP90A functions in protein folding, stabilization of signaling proteins, maintenance of proteostasis, and cellular responses to physiological and environmental stress. The prominent staining observed within muscle fibers is consistent with the substantial protein quality control and metabolic demands of contractile tissues. HIER was performed in pH 8.0 EDTA buffer. Tissue sections were blocked with 10% goat serum and incubated with primary antibody at 2 ug/ml overnight at 4°C prior to detection with HRP-conjugated secondary antibody and DAB chromogen.

Zebrafish HSP90AA1 Antibody WB. Western blot analysis of zebrafish head tissue lysate (lane 1), whole female zebrafish tissue lysate (lane 2), whole male zebrafish tissue lysate (lane 3), and zebrafish embryo tissue lysate (lane 4) using Zebrafish HSP90AA1 Antibody / Heat Shock Protein 90 Alpha Antibody demonstrates a prominent immunoreactive band at approximately 83-95 kDa, consistent with expression of HSP90A. HSP90A is a highly conserved molecular chaperone orthologous to human HSP90AA1 (heat shock protein 90 alpha family class A member 1) and functions in protein folding, stabilization of signaling proteins, maintenance of proteostasis, and cellular stress-response pathways. As one of the most abundant intracellular chaperones, HSP90A plays essential roles in embryonic development, signal transduction, and adaptation to physiological and environmental stress. Thirty micrograms of protein lysate were resolved under reducing conditions on a 10% SDS-PAGE gel and transferred to nitrocellulose prior to immunodetection. The observed bands support detection of zebrafish HSP90A by western blot analysis. Predicted molecular weight: ~83 kDa.