| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | HSPB1, HSP27, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, HSP28, MKBP, DMPK-binding protein |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Human HSP27 peptide |
| Isotype | |
| Product Type | |
| Reactivity | |
| Shipping | |
| Storage | |
| Target |
HSP25 (mouse) and its human homolog HSP27 are members of the small heat shock protein (sHSP) family, characterized by a conserved α-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.
A 1:5000 dilution of SMC-114 was sufficient for detection of HSP27 in 20 µg of HeLa cell lysate by ECL immunoblot analysis.
Cite this product varies by variant:
- SMC-114D — Size: 100 ug: HSP25/HSP27 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D, RRID: AB_2120775)
- SMC-114D-A390 — Size: 100 ug: HSP25/HSP27 Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-A390, RRID: AB_2697990)
- SMC-114D-A488 — Size: 100 ug: HSP25/HSP27 Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-A488, RRID: AB_2697991)
- SMC-114D-A594 — Size: 100 ug: HSP25/HSP27 Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-A594, RRID: AB_2697993)
- SMC-114D-APC — Size: 100 ug: HSP25/HSP27 Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-APC, RRID: AB_2697999)
- SMC-114D-BI — Size: 100 ug: HSP25/HSP27 Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-BI, RRID: AB_2698000)
- SMC-114D-FITC — Size: 100 ug: HSP25/HSP27 Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-FITC, RRID: AB_2698001)
- SMC-114D-HRP — Size: 100 ug: HSP25/HSP27 Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-HRP, RRID: AB_2698002)
- SMC-114D-PCP — Size: 100 ug: HSP25/HSP27 Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-PCP, RRID: AB_2698004)
- SMC-114D-RPE — Size: 100 ug: HSP25/HSP27 Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114D-RPE, RRID: AB_2698005)
- SMC-114S — Size: 12 ug: HSP25/HSP27 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-114S, RRID: AB_2120775)
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
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