Anti-Hsp90α Polyclonal Antibody for WB, IF/ICC, ELISA - P07900

Core Product Specifications and Parameters

Biological Background: Hsp90α Function and Localization

• Hsp90α (heat shock protein 90-alpha) is a molecular chaperone encoded by the HSP90AA1 gene, also known as HSP86, HSPC1, HSPCA, and LAP-2. It belongs to the HSP90 family of stress proteins that are highly conserved and ubiquitously expressed.
• Functions as a central chaperone that promotes the maturation, structural maintenance, and proper regulation of client proteins involved in cell cycle control and signal transduction. (PubMed:11274138, PubMed:12526792, PubMed:15577939) Related references: PMID:11274138, PMID:12526792, PMID:15577939
• Operates through an ATPase-dependent cycle that induces conformational changes in client proteins; dynamic interactions with co-chaperones modulate substrate recognition and chaperone activity. (PubMed:26991466, PubMed:27295069) Related references: PMID:26991466, PMID:27295069
• Plays a critical role in mitochondrial protein import by delivering preproteins to the mitochondrial import receptor TOMM70. (PubMed:12526792) Related references: PMID:12526792
• Modulates transcription at multiple levels: alters steady-state levels of transcription factors, influences epigenetic modifiers such as histone deacetylases, and participates in histone eviction from gene promoters to activate transcription. (PubMed:25973397) Related references: PMID:25973397
• Engages in immune and inflammatory responses by binding bacterial lipopolysaccharide (LPS) to promote TNF secretion, mediating antiviral signaling through TOMM70-IRF3/TBK1 association, and regulating TGF-beta signaling via STUB1 antagonism. (PubMed:11276205, PubMed:20628368, PubMed:25609812, PubMed:24613385) Related references: PMID:11276205, PMID:20628368, PMID:25609812, PMID:24613385
• Found in multiple subcellular compartments including the nucleus, cytoplasm, melanosome, cell membrane, and mitochondrion, reflecting its diverse functional roles.
• Post-translationally modified by acetylation, phosphorylation, S-nitrosylation, and ubiquitination, which regulate its activity and interactions.

Experimental Guidance and Technical Tips

• The immunogen corresponds to the C-terminal region (amino acids 433–732) of human Hsp90α; consider this when interpreting epitope accessibility in denaturing versus native assays.
• For Western blotting, the predicted molecular weight is 85 kDa, but endogenous Hsp90α may appear as additional bands due to post-translational modifications or isoform cross-reactivity; validate in your sample system.
• When using immunofluorescence/ICC, permeabilization is essential for intracellular detection; co-localization with organelle markers can help confirm subcellular distribution.
• For ELISA applications, test antibody pairing with appropriate capture/detection reagents; consider the polyclonal nature may require optimization of coating and blocking conditions.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers, research institutes, and laboratories with reliable access to IVD raw materials like this anti-Hsp90α polyclonal antibody, supporting studies in cancer biology, stress responses, and chaperone research. Our one-stop sourcing platform offers validated antibody pairs, optimized monoclonal and polyclonal antibodies, and bulk ancillary reagents to accelerate your assay development. We also specialize in rare target raw-material procurement, ensuring a seamless supply chain from concept to clinic.