SMC-114
HSP27 Antibody, Clone 8A7
Cannot supply to this region.
- SKU:
- SMC-114
- Additional Names:
- HSPB1, HSP27, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, HSP28, MKBP, DMPK-binding protein
- Application:
- Flow Cytometry, IHC, WB, IF, ICC, IP
- Concentration:
- 1 mg/ml
- Species Reactivity:
- Human
- Purification:
- Protein G Purified
- Storage Conditions:
- -20[o]C
- Supplier:
- StressMarq Biosciences
- Host:
- Mouse
- Reactivities:
- Bovine, Canine, Hamster, Human, Mouse, Rat, Guinea Pig, Ovine
- ABP:
- IMP-GEN-2015-06 < 10% Serum <100ml
- Buffer:
- PBS, 50% glycerol, 0.09% sodium azide
- Immunogen:
- Human HSP27 peptide
- Clone:
- 8A7
- Uniprot:
- P04792
- Synonyms:
- 28 kDa heat shock protein;CMT2F;epididymis secretory protein Li 102;estrogen-regulated 24 kDa protein;heat shock 27 kDa protein;heat shock 27kD protein 1;heat shock 27kDa protein 1;heat shock protein beta-1;HEL-S-102;HMN2B;HS.76067;Hsp25;HSP27;HSP28;putative heat shock protein family B member 1 isoform;SRP27;stress-responsive protein 27
- Extra Details:
- HSP25 (mouse) and its human homolog HSP27 are members of the small heat shock protein (sHSP) family, characterized by a conserved A Alpha-crystallin domain and a variable N-terminal region essential for oligomerization. These proteins form dynamic oligomers ranging from dimers to large multimers (8-40 monomers), with chaperone activity closely tied to their oligomeric state-larger assemblies exhibit potent anti-aggregation functions, while dimers are inactive. HSP27 is predominantly cytoplasmic under basal conditions but rapidly translocates to the nucleus in response to cellular stress, where it may stabilize nuclear structures and DNA. It is also rapidly phosphorylated in response to various stimuli, linking it to second messenger signaling pathways. Functionally, HSP27 acts as an ATP-independent molecular chaperone, preventing protein aggregation and stabilizing partially unfolded proteins, often in coordination with the HSP70 complex. In the nervous system, HSP27 plays a critical role in protecting neurons from proteotoxic stress, apoptosis, and oxidative damage-key features of neurodegenerative diseases such as Alzheimer's, Parkinson's, and ALS. It inhibits apoptotic signaling by blocking the cytochrome c/Apaf-1/procaspase-9 complex and may also influence cytoskeletal dynamics through interactions with actin and myosin. Upregulation of HSP27 correlates with increased phosphorylation and oligomer formation, suggesting a role in stress adaptation, cell differentiation, and potentially growth arrest. These properties make HSP27 a compelling target for therapeutic strategies aimed at enhancing neuronal resilience in neurodegenerative disease.
- Shipping Conditions:
- Blue Ice