Description
Background
The heat-shock proteins (HSPs) belong to a larger group of polypeptides, the stress proteins, that are induced in various combinations in response to environmental challenges and developmental transitions. Synthesis of the small (27-kD) HSP has been shown to be correlated with the acquisition of thermotolerance. The deduced 199-amino acid HSP27 protein shows sequence similarity to mammalian alpha-crystallins. Approximately 20% of its residues are susceptible to phosphorylation. The HSP27 gene, which is mapped to 7q11.23 and has 3 exons1, produced a 2.2-kb transcript in an in vitro transcription assay. Decreasing ROS in cells expressing mutant huntingtin, HSP27 protects cells against oxidative stress2. In other words, HSP27 is a suppressor of polyglutamine (polyQ)-mediated cell death3. Furthermore, MAPKAPK5 is a major stress-activated kinase that can phosphorylate HSP27 in vitro4.
Data Sheet
| Form | liquid |
| Ig type | rabbit IgG |
| Immunogen/Antigen | A synthetic peptide corresponding to a sequence at the C-terminal |
| Size | 100ug/vial |
| Storage | At -20C for one year. After reconstitution, at 4C for one month. |
