Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband®

Overview

This antibody is intended for detection of HSP90AA1 (Heat shock protein HSP 90-alpha) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.

Vendor notes: Boster Bio Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband® catalog # PB9635. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Monkey, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Antibody format: Rabbit Polyclonal Rabbit IgG
• Immunogen / epitope context: A synthetic peptide corresponding to a sequence at the C-terminus of human Hsp90 alpha, identical to the related mouse and rat sequences.
• Molecular weight context: reported MW: 90 kDa; calculated MW: 84660 MW
• Reactivity: Human,Monkey,Mouse,Rat
• Applications: Flow Cytometry, IF, IHC, ICC, WB

As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.

Biological background

Heat shock protein HSP 90-alpha; Heat shock protein HSP 90-alpha. Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene. The gene, HSP90AA1, encodes the human stress-inducible 90-kDa heat shock protein alpha (Hsp90A). Complemented by the constitutively expressed paralog Hsp90B which shares over 85% amino acid sequence identity, Hsp90A expression is initiated when a cell experiences proteotoxic stress. Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures. This molecular chaperoning ability of Hsp90A is driven by a cycle of structural rearrangements fueled by ATP hydrolysis. Current research on Hsp90A focuses in its role as a drug target due to its interaction with a large number of tumor promoting proteins and its role in cellular stress adaptation. Functional note: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. . Reported localization: Cytoplasm. Melanosome. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Expression/tissue context: Expressed in heart, skeletal muscle, eye and brain, and at much lower levels in some other tissues. .

Research relevance and current trends

• Cancer: Researchers commonly examine how HSP90AA1 (Heat shock protein HSP 90-alpha) relates to this theme using model systems and orthogonal readouts.
• Chaperones: Researchers commonly examine how HSP90AA1 (Heat shock protein HSP 90-alpha) relates to this theme using model systems and orthogonal readouts.
• Heat Shock Proteins: Researchers commonly examine how HSP90AA1 (Heat shock protein HSP 90-alpha) relates to this theme using model systems and orthogonal readouts.

Common research applications

• Western blotting: compare relative HSP90AA1 (Heat shock protein HSP 90-alpha) levels across conditions; band patterns may reflect isoforms and processing.
• IHC/IHC-F: assess spatial distribution of HSP90AA1 (Heat shock protein HSP 90-alpha) across tissue regions and cell types using matched controls.
• IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
• Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.

Notes for experimental interpretation

• Specificity notes: No cross reactivity with other proteins.
• Cross-reactivity: No cross-reactivity with other proteins
• Family / similarity context: Contains 1 HMG box DNA-binding domain.
• Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
• Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.