Anti-HSP27 (Ab-78) Antibody

Raised in rabbit against the human 27 kDa heat shock protein HSP27 (also called HSPB1), this polyclonal antibody from Antibodies.com recognizes the small stress-response chaperone in both its unmodified and post-translationally modified states. The unconjugated format lets researchers pair the reagent with HRP, fluorophore, or biotin secondary antibodies of their choice, and the 100 µL volume is supplied in a single vial suited to routine western blot and immunohistochemistry workflows.

Validated for WB and IHC on human samples, the reagent reveals the protein in cell lysates, tissue homogenates, and formalin-fixed paraffin-embedded sections. HSP27 functions as an ATP-independent molecular chaperone that holds partially folded client proteins, remodels the actin cytoskeleton, and modulates apoptosis through interactions with cytochrome c and procaspase-3. Phosphorylation at serine residues including Ser15, Ser78, and Ser82 by MAPKAPK2/3 reorganizes HSP27 between large oligomeric assemblies and smaller dimers, providing a widely used readout of p38 MAPK pathway engagement during heat shock, oxidative, and cytokine stress.

Common research applications include profiling chaperone responses in tumor cells, examining neuroprotective signaling in neurodegeneration models, monitoring cardioprotection in ischemia-reperfusion studies, and tracking cytoskeletal remodeling during cell migration. Because the reagent is polyclonal rather than monoclonal, it recognizes multiple epitopes across the HSP27 sequence, which improves the chance of detecting the protein even when one site is masked by phosphorylation or fixation-induced crosslinking. For handling, antibody stocks are typically aliquoted and frozen at -20 °C, with working dilutions refrigerated and protected from repeated freeze-thaw cycles to preserve titer.