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HSP90 Protein

CAT: 0400-SPR-122ASize: 50 µgDry Ice: NoHazardous: No
CAT#:0400-SPR-122ASize:50 µg
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AVAILABILITY: InStock
24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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Background
HSP90 is a highly conserved and abundantly expressed molecular chaperone that exists in two major cytosolic isoforms: HSP90α and HSP90β. It is essential for the folding, stabilization, and functional regulation of a wide array of client proteins, many of which are involved in signal transduction, cell cycle control, and stress responses. In the nervous system, HSP90 plays a critical role in maintaining proteostasis, particularly under conditions of cellular stress. It forms dynamic complexes with co-chaperones such as CDC37, p23, and immunophilins, which guide the maturation and stabilization of client proteins. This function is especially relevant in neurodegenerative diseases, where protein misfolding and aggregation are central pathological features. HSP90 has been shown to interact with key neurodegenerative disease-related proteins, including tau, α-synuclein, and huntingtin. While it can stabilize these proteins and prevent aggregation, it may also inadvertently preserve toxic conformers. As such, HSP90 is a double-edged sword in neurodegeneration—both protective and potentially pathogenic. Pharmacological inhibition of HSP90 has emerged as a therapeutic strategy to promote the degradation of misfolded proteins and restore cellular homeostasis. Its high expression in neurons and involvement in multiple neurodegenerative pathways make HSP90 a compelling target for therapeutic intervention and biomarker development.
Description
P. Falciparum Recombinant HSP90 Partial Protein
Product Name Alternative
HSP90, HSP90AB1, HSP90-beta, HSPCB, HSPC2, Heat shock protein HSP 90-beta, Heat shock 84 kDa protein, HSP84, HSP90B
UNSPSC
12352202
UN Code
Non-hazardous
Hazard Statement
Non-hazardous
Gene ID
811999
Swiss Prot
Q8IL32
Accession Number
XP_001348591.1
Cellular Locus
Cytoplasm | Melanosome
Expression System
E. coli
Host
E. coli
Origin Species
P. falciparum
Target
HSP90
Conjugation
No tag
Nature
Recombinant
Sequence
QPVLEINPNHFIIKQLNHLIQIDKMNLQNSEIAEQIFDVASMQGGYTIDDTGLFAKRVIGMMEKNAEQYLMNVQSNISNNTLNNNTSGSEMPQNNSPNELQSEMKSTNGIDDNSNISENKINESSSNQNNIGENSIAEENNIKNIAESDVNKINLGENDVSQNTMHKQDSGLFNLDPSILNSNMLSGSDKTLL
Applications
WB | SDS-PAGE
Field of Research
Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
Purification Method
Affinity Purified
Purification
Affinity Purified
Limit Of Detection
This product has been certified >90% pure using SDS-PAGE analysis.
Concentration
Lot/batch specific. See included datasheet.
Purity
>90%
Weight
0.05
Length
Partial
Buffer
50mM Tris/HCl pH7.5, 300mM NaCl, 10% glycerol
Molecular Weight
~21.4 kDa
Precautions
Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
References & Citations
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.
Shipping Conditions
Blue Ice or 4ºC
Storage Conditions
-20ºC
Protein Length
Partial
Background Reference 01
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.
Location
Cytoplasm | Melanosome
AA Sequence
QPVLEINPNHFIIKQLNHLIQIDKMNLQNSEIAEQIFDVASMQGGYTIDDTGLFAKRVIGMMEKNAEQYLMNVQSNISNNTLNNNTSGSEMPQNNSPNELQSEMKSTNGIDDNSNISENKINESSSNQNNIGENSIAEENNIKNIAESDVNKINLGENDVSQNTMHKQDSGLFNLDPSILNSNMLSGSDKTLL
Immunogen Species
P. falciparum
Product MSDS
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