HSP90 alpha Antibody, Clone Hyb-K41009: ATTO 488

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.

HSP90AA1, HSP90-alpha, HSP90A, HSPCA, HSPC1, Heat shock protein HSP 90-alpha, Heat shock 90 kDa protein 1 alpha isoform, HSPCAL3, HSP86, HSP89A, HSP90Alpha

1 µg/ml of SMC-108 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.

1. Nemoto, T. et al. (1997) J.Biol Chem. 272: 26179-26187. 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.

1. Nemoto, T. et al. (1997) J.Biol Chem. 272: 26179-26187. 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.