Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband®

Overview

Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband® is an antibody targeting HSP90AA1. Common applications include WB, IHC, ICC, IF, Flow Cytometry, ELISA. Key specifications include host: Rabbit; clonality: Polyclonal; isotype: Rabbit IgG; reactivity: Human,Mouse,Rat; observed MW: 95 kDa; calculated MW: 84660 MW.

Boster Bio Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband® catalog # PB9089. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, 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

• Target: HSP90AA1 — Heat shock protein HSP 90-alpha
• Antibody format: Host: Rabbit; Clonality: Polyclonal; Isotype: Rabbit IgG
• Species reactivity: Human,Mouse,Rat
• Molecular weight guidance: Observed: 95 kDa; Calculated: 84660 MW

Specificity note: No cross reactivity with other proteins.

Biological background

Protein function (datasheet): 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. .

Scientific background (datasheet): 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.

Cellular localization (datasheet): Cytoplasm. Melanosome. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Tissue details (datasheet): Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non- proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle). .

Sequence similarities (datasheet): Contains 1 RHD (Rel-like) domain.

Research relevance and current trends

• Commonly studied in contexts related to Cancer,Chaperones,Heat Shock Proteins,Protein Trafficking,Signal Transduction,Tumor Biomarkers.
• Supports comparative expression analysis across conditions, genotypes, or treatments when paired with appropriate controls.
• Useful for confirming target presence and subcellular distribution using orthogonal readouts (e.g., microscopy vs. immunoblotting).

Common research applications

• Western blot (WB): Compare relative target abundance and apparent size/isoforms across samples; interpret bands in light of expected MW and potential PTMs.
• ELISA: Measure target abundance in compatible matrices using a standard-curve readout; ensure dilution linearity and appropriate controls.
• Immunohistochemistry (IHC): Assess tissue distribution and cell-type patterns; interpret staining with appropriate negative controls and antigen context.
• Immunofluorescence / ICC: Visualize subcellular localization and co-localization patterns; consider fixation/permeabilization compatibility and controls.
• Flow cytometry: Quantify target-positive populations in single-cell suspensions; pair with viability and isotype/FMO controls conceptually.

Notes for experimental interpretation

• Consider isoforms, post-translational modifications, and processing that can shift apparent molecular weight or localization.
• Cross-reactivity (datasheet): No cross-reactivity with other proteins
• Use appropriate positive and negative controls (e.g., KO/KD, blocking peptide, or isotype controls) to support specificity interpretation.

As a polyclonal antibody, this reagent may recognize multiple epitopes on the target, which can improve detection robustness but may require careful specificity controls.

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.