HSP90AA1 / HSP90 Protein

Heat Shock Protein HSP 90-alpha Protein

HSP90AA1 / HSP90 Protein Product Information

• Synonym: HSP90AA1,FLJ31884, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP2
• Protein Construction: A DNA sequence encoding the human HSP90 isoform 2 (NP_005339.3) C-terminal segment , corresponding to amino acid sequence ( Glu 535-Asp 732 ) was expressed and purified, with two additonal aa ( Gly & Pro ) at the N terminus
• Source: Human
• Expression Host: E. coli

HSP90AA1 / HSP90 Protein QC Testing

• Purity: > 97 % as determined by SDS-PAGE
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Gly
• Molecular Mass: The recombinant human HSP90 (aa 535-732) consisting of 200 amino acids and has a calculated molecular mass of 22.6 KDa. It migrates as an 24 kDa band in SDS-PAGE under reducing conditions
• Formulation: Lyophilized from sterile PBS , pH 7.4
• SDS-PAGE: HSP90 protein

HSP90AA1 / HSP90 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

HSP90AA1 / HSP90 Protein Description

Heat shock protein HSP 90-alpha, also known as Heat shock 86 kDa, Renal carcinoma antigen NY-REN-38, HSP90AA1 and HSP90A, is a cytoplasm protein which belongs to theheat shock protein 90 family. The molecular chaperone HSP90/HSP90AA1 has emerged as an important target in cancer treatment because of its roles in maintaining transformation and regulating the function of proteins involved in apoptotic, survival and growth pathways. Many HSP90 inhibitors function by binding to the N-terminal ATP pocket, but the chaperone has many other vulnerable points. Agents that interact with its C-terminus or modify its post-translational status represent additional ways of interfering with HSP90 chaperone activity. HSP90/HSP90AA1 is a highly conserved and very abundant protein in the cytosol of both eukaryotic and prokaryotic cells. HSP90/HSP90AA1 acts in concert with several other heat shock and non heat shock proteins to mediate important regulatory effects. These roles of Hsp90 leave unexplained its high abundance and heat shock regulation. HSP90/HSP90AA1 has been identified as an ATP independent molecular chaperone, which binds transiently to folding intermediates and prevents aggregation and supports the refolding of the intermediates to the native state. The finding that HSP90 interacts with late, probably highly structured, folding intermediates led to the suggestion that HSP90 might function as a general chaperone for well structured not yet native polypeptides.

References

1. Jakob,U. 1996, Front Biosci. 1 : d309-17.
2. Nemoto T.et al., 1995, Eur. J. Biochem. 233:1-8.
3. Young J.C. et al., 1998, J. Biol. Chem. 273:18007-10 
4. Chiosis,G. et al., 2004,  Drug Discov Today.  9 (20):881-8.
5. Richter,K. et al., 2007,Nat Struct Mol Biol 14 (2):90-4.