Mouse Monoclonal HSP90AB1 Antibody

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     Red: Control Antigen (100ng); Purple: Antigen (10ng); Green: Antigen (50ng); Blue: Antigen (100ng);    

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     Western blot analysis using HSP90AB1 mouse mAb against Jurkat (1), A431 (2), Hela (3), A549 (4), HEK293 (5), K562 (6), NIH/3T3 (7), PC-12 (8) and Cos7 (9) cell lysate.    

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     Immunofluorescence analysis of Hela cells using HSP90AB1 mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor-555 phalloidin.    

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     Flow cytometric analysis of Hela cells using HSP90AB1 mouse mAb (green) and negative control (purple).    

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     Immunohistochemical analysis of paraffin-embedded human kidney cancer tissues (left) and brain tissues (right) using HSP90AB1 mouse mAb with DAB staining.    

HSP90AB1 is a member of the heat shock protein 90 (HSP90) family, a highly conserved group of molecular chaperones critical for maintaining cellular homeostasis. Specifically, HSP90AB1 encodes the cytosolic isoform HSP90β, which, along with HSP90α (encoded by HSP90AA1), plays a central role in stabilizing and folding client proteins, many of which are involved in signal transduction, cell cycle regulation, and stress response. Unlike HSP90α, HSP90AB1 is constitutively expressed under normal conditions and further induced by cellular stress, such as heat shock or hypoxia.

Antibodies targeting HSP90AB1 are widely used in research to study its expression, localization, and interaction with client proteins or co-chaperones. These tools are essential for techniques like Western blotting (WB), immunohistochemistry (IHC), and immunoprecipitation (IP). Given HSP90's association with cancer progression—due to its role in stabilizing oncogenic clients like HER2. AKT, and mutant p53—HSP90AB1 antibodies are particularly valuable in oncology research. They help investigate HSP90 overexpression in tumors, evaluate the efficacy of HSP90 inhibitors (e.g., geldanamycin derivatives), and explore mechanisms of drug resistance.

However, researchers must ensure antibody specificity, as HSP90 isoforms (α/β) share ~85% sequence identity. Cross-reactivity can lead to misinterpretation, necessitating validation via isoform-specific controls. Studies using HSP90AB1 antibodies have also shed light on its non-canonical roles, including extracellular signaling in wound healing and immune modulation. Overall, these antibodies remain pivotal in dissecting HSP90β's multifaceted contributions to cellular physiology and disease.