| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | HSP90AA1, HSP90-alpha, HSP90A, HSPCA, HSPC1, Heat shock protein HSP 90-alpha, Heat shock 90 kDa protein 1 alpha isoform, HSPCAL3, HSP86, HSP89A, HSP90Alpha |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Recombinant Full Length Human HSP90alpha Protein |
| Isotype | |
| Product Type | |
| Reactivity | |
| Shipping | |
| Storage | |
| Target |
HSP90α is a cytosolic isoform of the highly conserved heat shock protein 90 (HSP90) family, which plays a central role in maintaining protein homeostasis under both normal and stress conditions. Although HSP90α and its isoform HSP90β share 85% sequence identity, HSP90α predominantly forms homodimers and is more dynamically regulated in response to cellular stress.
In the nervous system, HSP90α is essential for the folding, maturation, and stabilization of a wide range of client proteins, many of which are involved in synaptic signaling, neuronal survival, and stress response. These include kinases (e.g., c-Raf), transcription factors (e.g., p53), and hormone receptors—proteins that are often dysregulated in neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s disease.
HSP90α functions as part of a multi-protein chaperone complex, interacting with co-chaperones like Cdc37 and p23. Upon ATP binding, HSP90α undergoes conformational changes that enable it to stabilize client proteins and prevent their degradation. However, in disease contexts, this protective mechanism can inadvertently preserve toxic protein species, contributing to pathogenesis.
Pharmacological inhibition of HSP90α—using agents like geldanamycin—has shown promise in disrupting these pathogenic interactions and restoring proteostasis in neurodegenerative models.
0.5 µg/ml of SMC-147 was sufficient for detection of HSP90alpha in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Cite this product varies by variant:
- SMC-147B — Size: 200 ug: HSP90 alpha Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B, RRID: AB_2120931)
- SMC-147B-A390 — Size: 200 ug: HSP90 alpha Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-A390, RRID: AB_2698364)
- SMC-147B-A488 — Size: 200 ug: HSP90 alpha Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-A488, RRID: AB_2698365)
- SMC-147B-A594 — Size: 200 ug: HSP90 alpha Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-A594, RRID: AB_2698367)
- SMC-147B-APC — Size: 200 ug: HSP90 alpha Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-APC, RRID: AB_2698373)
- SMC-147B-BI — Size: 200 ug: HSP90 alpha Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-BI, RRID: AB_2698374)
- SMC-147B-FITC — Size: 200 ug: HSP90 alpha Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-FITC, RRID: AB_2698375)
- SMC-147B-HRP — Size: 200 ug: HSP90 alpha Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-HRP, RRID: AB_2698376)
- SMC-147B-PCP — Size: 200 ug: HSP90 alpha Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-PCP, RRID: AB_2698378)
- SMC-147B-RPE — Size: 200 ug: HSP90 alpha Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147B-RPE, RRID: AB_2698379)
- SMC-147S — Size: 12 ug: HSP90 alpha Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-147S, RRID: AB_2120931)
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. Minami, Y, et al. (1991), J.Biol Chem. 266: 10099-10103.
3. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.
4. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186.
5. Neckers L, et al. (2002) Trends Mol Med 8: S55-S61.
6. Pratt W, Toft D. (2003) Exp Biol Med 228: 111-133.
7. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360.
8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.
9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.
10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5): 881-889.
