| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | HSPB1, HSP27, HSP25, HSP28, Heat shock protein beta-1, Heat shock 27 kDa protein, MKBP, DMPK-binding protein, SRP27, 28kDa heat shock protein, CMT2F |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Full length human HSP27 |
| Isotype | |
| Product Type | |
| Reactivity | |
| Shipping | |
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| Target |
HSP27, a member of the small heat shock protein (sHSP) family, is an abundant and ubiquitously expressed molecular chaperone found in both normal and cancerous human cells. Structurally, HSP27 features a conserved α-crystallin domain at the C-terminus and a less conserved N-terminal WD/EPF domain, which is essential for forming high-molecular-weight oligomers. These oligomers, composed of 8–40 monomers, are critical for HSP27’s chaperone activity—larger assemblies exhibit strong anti-aggregation properties, while dimers are inactive.
Under non-stress conditions, HSP27 resides in the cytoplasm but rapidly translocates to the nucleus in response to cellular stress, where it may help stabilize DNA and nuclear membranes. Functioning as an ATP-independent chaperone, HSP27 prevents protein aggregation and stabilizes partially unfolded proteins, facilitating their refolding via the HSP70 complex.
In neuroscience, HSP27 is increasingly recognized for its role in protecting neurons from proteotoxic stress, oxidative damage, and apoptosis—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.
HSP27 expression is tightly regulated by phosphorylation, which promotes the formation of large, active oligomers. Its involvement in stress response, apoptosis inhibition, and cell differentiation highlights its therapeutic potential in neurodegenerative disease research and intervention.
0.5 µg/ml of SMC-161 was sufficient for detection of HSP27 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Cite this product varies by variant:
- SMC-161B — Size: 200 ug: HSP27 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B, RRID: AB_2248586)
- SMC-161B-A390 — Size: 200 ug: HSP27 Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-A390, RRID: AB_2698585)
- SMC-161B-A488 — Size: 200 ug: HSP27 Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-A488, RRID: AB_2698586)
- SMC-161B-A594 — Size: 200 ug: HSP27 Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-A594, RRID: AB_2698588)
- SMC-161B-APC — Size: 200 ug: HSP27 Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-APC, RRID: AB_2698594)
- SMC-161B-BI — Size: 200 ug: HSP27 Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-BI, RRID: AB_2698595)
- SMC-161B-FITC — Size: 200 ug: HSP27 Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-FITC, RRID: AB_2698596)
- SMC-161B-HRP — Size: 200 ug: HSP27 Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-HRP, RRID: AB_2698597)
- SMC-161B-PCP — Size: 200 ug: HSP27 Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-PCP, RRID: AB_2698599)
- SMC-161B-RPE — Size: 200 ug: HSP27 Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161B-RPE, RRID: AB_2698600)
- SMC-161S — Size: 12 ug: HSP27 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-161S, RRID: AB_2248586)
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.
2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56.
3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229.
4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70.
5. Sarto C., Binnz P.A., and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26.
6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.
