HSP90 (P. falciparum) Antibody

HSP90 is a highly conserved and abundantly expressed molecular chaperone that plays a central role in protein folding, stabilization, and cellular signaling. In Plasmodium falciparum, the parasite responsible for the most lethal form of human malaria, HSP90 is essential for parasite survival and adaptation to host-induced stress. The parasite expresses two major cytosolic isoforms—PfHSP90α and PfHSP90β—which share 85% sequence identity but differ in oligomeric structure and function. Despite being classified as a heat shock protein, PfHSP90 is constitutively expressed at high levels, even in unstressed conditions, and supports the folding and maturation of key regulatory proteins. These include kinases, transcription factors, and other signaling molecules critical for parasite development and virulence. In neuroscience and neurodegenerative disease research, HSP90 has gained attention for its dual role: stabilizing misfolded proteins and, paradoxically, protecting pathogenic proteins from degradation. This duality is mirrored in P. falciparum, where PfHSP90 may similarly buffer proteotoxic stress, making it a compelling target for antimalarial strategies inspired by neurodegenerative disease mechanisms. HSP90 (P. falciparum) Antibody enables specific detection of PfHSP90 in parasite lysates and infected cells, supporting studies on chaperone function, stress response, and drug targeting in malaria.

HSP90, Heat shock protein 90, Heat shock protein 90 kDa, PF14_0417, PF3D7_1465900, HSP90_PLAFA, Heat shock 86 kDa protein, heat shock 90kDa protein 1 alpha, Heat shock protein 90kDa alpha cytosolic class A member 1, Heat shock protein 90kDa alpha cytosolic class B member 1, Heat shock protein HSP 90 alpha, Heat shock protein HSP 90 beta, Heat shock protein HSP 90-alpha, HSP 84, HSP 86, HSP 90, HSP90 Beta, HSP90A, HSP90AA1, HSP90AB1, HSP90B, HSP90N, HSPC1, HSPC2, HSPCA, HSPCAL1, HSPCAL4, HSPCB, HSPN

0.7 µg/ml of SPC-187 was sufficient for detection of PfHSP90 in 20 µg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit 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 S.J.H., 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 W.B. (1998) Proc Soc Exptl Biol Med. 217: 420–434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 8324–8328. 10. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278 (20) : 18336-45. 11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279 (45) :46692-9.