Anti-Hsp90β Polyclonal Antibody for WB, IHC-P, IF/ICC, ELISA - P08238

Core Product Specifications and Parameters

Biological Background: Hsp90β Function and Localization

• HSP90-beta (Hsp90β, HSP84, HSPC2, HSPCB) is a member of the heat shock protein 90 family, an abundant molecular chaperone with key roles in protein folding, stability, and signal transduction.
• The chaperone cycle is driven by ATP binding and hydrolysis, inducing conformational changes in client proteins. HSP90 interacts with co-chaperones that modulate substrate recognition and cycle progression (PubMed:16478993, PubMed:19696785, PubMed:26991466, PubMed:27295069).
  Related references:
  PMID:16478993, PMID:19696785, PMID:26991466, PMID:27295069
• HSP90 contributes to transcriptional regulation by altering transcription factor steady-state levels, modulating epigenetic modifiers, and facilitating histone eviction from gene promoters (PubMed:25973397).
  Related references:
  PMID:25973397
• It antagonizes STUB1-mediated inhibition of TGF-beta signaling by blocking SMAD3 ubiquitination and degradation (PubMed:24613385).
  Related references:
  PMID:24613385
• Through chaperoning BIRC2, HSP90 promotes cell differentiation and protects BIRC2 from proteasomal degradation (PubMed:18239673).
  Related references:
  PMID:18239673
• Under heat shock, HSP90 facilitates STAT1 phosphorylation by chaperoning JAK2 and PRKCE, and in turn activates its own transcription in a positive feedback loop (PubMed:20353823).
  Related references:
  PMID:20353823
• HSP90 mediates the ERGIC translocation of leaderless secretory cargos such as interleukin-1 (IL-1) via interaction with the cargo receptor TMED10 (PubMed:32272059).
  Related references:
  PMID:32272059
• During N. meningitidis infection, HSP90 binds the adhesin NadA, stimulating monocytes and interfering with bacterial invasion (PubMed:21949862).
  Related references:
  PMID:21949862
• Subcellular localization includes cytoplasm, nucleus, melanosome, cell membrane, and secreted fractions; it is subject to post‑translational modifications such as acetylation, phosphorylation, methylation, and ubiquitination.

Experimental Guidance and Technical Tips

• The immunogen corresponds to the N‑terminal region (aa 1–300) of human Hsp90β; the antibody may be particularly suitable for detecting full-length endogenous Hsp90β and N‑terminal fragments.
• For Western blotting, a band near 83 kDa is expected; reduce/denature conditions should be optimized empirically.
• In immunohistochemistry and immunocytochemistry, verify signal specificity by including isotype controls and, where possible, antigen pre‑absorption.
• When using for ELISA, consider pairing with a detection antibody that recognizes a distinct epitope to avoid competition.
• Cross‑reactivity with mouse and rat Hsp90β has been reported; however, validate performance in the target tissue or cell line of interest.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio serves as a comprehensive sourcing partner for IVD raw materials, streamlining access to validated antibody pairs, optimized polyclonal antibodies like this anti‑Hsp90β, and bulk ancillary reagents. Whether your project focuses on cellular stress signaling, cancer biology, or chaperone‑mediated pathways, CamelBio can supply high‑quality components to support your diagnostic or research applications. From concept to clinic, we help bridge supply gaps for routine and rare‑target raw materials.