Antigen Description
Heat shock proteins are ubiquitous proteins and have been characterized as cytoprotective molecular chaperones. The typical function of a chaperone is to assist a protein to attain its functional conformation to prevent non-functional aggregation of misfolded proteins. The principal HSP families are HSP90, HSP70, HSP60 and the small HSPs including HSP27, ubiquitin, α-crystallin, Hsp20 and others. The common functions of small Hsps are chaperone activity, thermotolerance, inhibition of apoptosis, regulation of cell development, and cell differentiation. Hsp27 has a molecular weight of approximately 27 kDa, although it has been shown to form large aggregates of up to 800 kDa in the cytosol. Hsp27 is found in several types of human cells, including tumour cells. Hsp27 interferes with apoptosis through its ability to interact with and inhibit key components of the apoptotic signaling pathway, including the caspase activation complex. Over expression of heat shock proteins can increase the tumorigenic potential of tumour cells. HSP27 also has been reported to be involved in development and progression of hormone-refractory prostate cancer.
Pathway
Amoebiasis; Destabilization of mRNA by AUF1 (hnRNP D0); FAS pathway and Stress induction of HSP regulation; IL-3 Signaling Pathway; IL-6 Signaling Pathway; MAPK signaling pathway; Metabolism; Metabolism of RNA; Metabolism of Mrna; Regulation of mRNA Stability by Proteins that Bind AU-rich Elements; Signaling events mediated by VEGFR1 and VEGFR2; Signaling mediated by p38-alpha and p38-beta; TNF-alpha/NF-kB Signaling Pathway; VEGF signaling pathway; p38 MAPK Signaling Pathway; p38 signaling media
COA
Publication 
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