Description
Background
Hsp90 (heat shock protein 90) is a molecular chaperone and is one of the most abundant proteins expressed in cells.[1] It is a member of the heat shock protein family which is upregulated in response to stress. Hsp90 is found in bacteria and all branches of eukarya, but it is apparently absent in archaea.[2] Cytoplasmic Hsp90 is essential for viability under all conditions in eukaryotes, the bacterial homologue HtpG is dispensable under non-heat stress conditions.[3]The function of Hsp90 includes assisting in protein folding, cell signaling, and tumor repression. This protein was first isolated by extracting proteins from stressed cells. These cells were stressed by heating, dehydrating or by other means, all of which caused the cell’s proteins to begin to denature.[4] Researchers later realized that Hsp90 has other essential functions in unstressed cells.
Data Sheet
| Form | lyophilized |
| Ig type | rabbit IgG |
| Immunogen/Antigen | A synthetic peptide corresponding to a sequence at the C-terminal |
| Reconstitution | 0.2ml of distilled water will yield a concentration of 500μg/ml. |
| Size | 100ug/vial |
| Storage | At -20C for one year. After reconstitution, at 4C for one month. |
