Phospho-HSP27/HSPB1-S82 Rabbit pAb - P04792

Core Product Specifications and Parameters

Biological Background: HSP27/HSPB1 Function and Localization

• Heat shock protein beta-1 (HSPB1), also known as HSP27, is a member of the small heat shock protein family encoded by the HSPB1 gene in humans.
• Functions as a molecular chaperone that maintains denatured proteins in a folding-competent state, playing a critical role in cellular proteostasis.
  Related references: PMID:10383393, PMID:20178975
• Plays a key role in stress resistance and actin organization, contributing to cytoskeletal stability and cell survival under adverse conditions.
  Related references: PMID:19166925
• Through its chaperone activity, regulates the phosphorylation and axonal transport of neurofilament proteins, implicating it in neuronal function and neurodegeneration.
  Related references: PMID:23728742
• Localizes to the cytoplasm, nucleus, and cytoskeleton/spindle, reflecting its dynamic involvement in various cellular processes.
• Ubiquitously expressed in tissues, with highest levels in heart and striated/smooth muscle, as well as in serum and cerebrospinal fluid.
• A phosphoprotein subject to post-translational modifications, including phosphorylation at Ser82, which modulates its chaperone activity and cellular localization.
• Associated with Charcot-Marie-Tooth disease and other neuropathies, highlighting its disease relevance.

Experimental Guidance and Technical Tips

• For Western blot, validate the phospho-specific signal by treating samples with phosphatase or comparing with a non-phosphorylated peptide blocking control.
• In IHC-P, consider antigen retrieval conditions and verify staining specificity in known positive tissues such as heart or muscle.
• For immunoprecipitation, optimize antibody concentration and verify the immunoprecipitated band by mass spectrometry or western blot with a total HSP27 antibody.
• Be aware that HSP27 may form oligomers, which could affect migration patterns; the predicted monomeric weight is ~23 kDa, but phosphorylated or modified forms may shift.
• Due to cross-reactivity being human, if extending to other species, validate sequence homology around the phosphorylation site.

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